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Journal articles on the topic 'KIF5'

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Published: 4 June 2021
Last updated: 15 February 2022

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1

Aizawa, H., Y. Sekine, R. Takemura, Z. Zhang, M. Nangaku, and N. Hirokawa. "Kinesin family in murine central nervous system." Journal of Cell Biology 119, no. 5 (December 1, 1992): 1287–96. http://dx.doi.org/10.1083/jcb.119.5.1287.

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In neuronal axons, various kinds of membranous components are transported along microtubules bidirectionally. However, only two kinds of mechanochemical motor proteins, kinesin and brain dynein, had been identified as transporters of membranous organelles in mammalian neurons. Recently, a series of genes that encode proteins closely related to kinesin heavy chain were identified in several organisms including Schizosaccharomyces pombe, Aspergillus niddulans, Saccharomyces cerevisiae, Caenorhabditus elegans, and Drosophila. Most of these members of the kinesin family are implicated in mechanisms of mitosis or meiosis. To address the mechanism of intracellular organelle transport at a molecular level, we have cloned and characterized five different members (KIF1-5), that encode the microtubule-associated motor domain homologous to kinesin heavy chain, in murine brain tissue. Homology analysis of amino acid sequence indicated that KIF1 and KIF5 are murine counterparts of unc104 and kinesin heavy chain, respectively, while KIF2, KIF3, and KIF4 are as yet unidentified new species. Complete amino acid sequence of KIF3 revealed that KIF3 consists of NH2-terminal motor domain, central alpha-helical rod domain, and COOH-terminal globular domain. Complete amino acid sequence of KIF2 revealed that KIF2 consists of NH2-terminal globular domain, central motor domain, and COOH-terminal alpha-helical rod domain. This is the first identification of the kinesin-related protein which has its motor domain at the central part in its primary structure. Northern blot analysis revealed that KIF1, KIF3, and KIF5 are expressed almost exclusively in murine brain, whereas KIF2 and KIF4 are expressed in brain as well as in other tissues. All these members of the kinesin family are expressed in the same type of neurons, and thus each one of them may transport its specific organelle in the murine central nervous system.
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2

Matsuzaki, Fumiko, Michiko Shirane, Masaki Matsumoto, and Keiichi I. Nakayama. "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation." Molecular Biology of the Cell 22, no. 23 (December 2011): 4602–20. http://dx.doi.org/10.1091/mbc.e11-01-0068.

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Neurons are highly polarized cells with long neurites. Vesicular transport is required for neurite extension. We recently identified protrudin as a key regulator of vesicular transport during neurite extension. Expression of protrudin in nonneuronal cells thus induces formation of neurite-like membrane protrusions. We adopted a proteomics approach to identify proteins that associate with protrudin. Among the protrudin-associated proteins, including many with a function related to intracellular trafficking, we focused on KIF5, a motor protein that mediates anterograde vesicular transport in neurons. A coimmunoprecipitation assay confirmed that endogenous protrudin and KIF5 interact in mouse brain. Overexpression of KIF5 induced the formation of membrane protrusions in HeLa cells, reminiscent of the effect of protrudin overexpression. Forced expression of both protrudin and KIF5 promoted protrusion extension in a synergistic manner, whereas depletion of either protein attenuated protrusion formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin–KIF5 complex contributes to the transport of these proteins in neurons. Given that mutation of protrudin or KIF5 is a cause of human hereditary spastic paraplegia, the protrudin–KIF5 axis appears to be integral to neuronal function.
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3

Takemura, R., T. Nakata, Y. Okada, H. Yamazaki, Z. Zhang, and N. Hirokawa. "mRNA expression of KIF1A, KIF1B, KIF2, KIF3A, KIF3B, KIF4, KIF5, and cytoplasmic dynein during axonal regeneration." Journal of Neuroscience 16, no. 1 (January 1, 1996): 31–35. http://dx.doi.org/10.1523/jneurosci.16-01-00031.1996.

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4

Nakata, Takao, Shinsuke Niwa, Yasushi Okada, Franck Perez, and Nobutaka Hirokawa. "Preferential binding of a kinesin-1 motor to GTP-tubulin–rich microtubules underlies polarized vesicle transport." Journal of Cell Biology 194, no. 2 (July 18, 2011): 245–55. http://dx.doi.org/10.1083/jcb.201104034.

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Polarized transport in neurons is fundamental for the formation of neuronal circuitry. A motor domain–containing truncated KIF5 (a kinesin-1) recognizes axonal microtubules, which are enriched in EB1 binding sites, and selectively accumulates at the tips of axons. However, it remains unknown what cue KIF5 recognizes to result in this selective accumulation. We found that axonal microtubules were preferentially stained by the anti–GTP-tubulin antibody hMB11. Super-resolution microscopy combined with EM immunocytochemistry revealed that hMB11 was localized at KIF5 attachment sites. In addition, EB1, which binds preferentially to guanylyl-methylene-diphosphate (GMPCPP) microtubules in vitro, recognized hMB11 binding sites on axonal microtubules. Further, expression of hMB11 antibody in neurons disrupted the selective accumulation of truncated KIF5 in the axon tips. In vitro studies revealed approximately threefold stronger binding of KIF5 motor head to GMPCPP microtubules than to GDP microtubules. Collectively, these data suggest that the abundance of GTP-tubulin in axonal microtubules may underlie selective KIF5 localization and polarized axonal vesicular transport.
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5

Nakata, Takao, and Nobutaka Hirokawa. "Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head." Journal of Cell Biology 162, no. 6 (September 15, 2003): 1045–55. http://dx.doi.org/10.1083/jcb.200302175.

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Post-Golgi carriers of various newly synthesized axonal membrane proteins, which possess kinesin (KIF5)-driven highly processive motility, were transported from the TGN directly to axons. We found that KIF5 has a preference to the microtubules in the initial segment of axon. Low dose paclitaxel treatment caused missorting of KIF5, as well as axonal membrane proteins to the tips of dendrites. Microtubules in the initial segment of axons showed a remarkably high affinity to EB1–YFP, which was known to bind the tips of growing microtubules. These findings revealed unique features of the microtubule cytoskeletons in the initial segment, and suggested that they provide directional information for polarized axonal transport.
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6

Chen, Ying-Chun, Hao-Ru Huang, Chia-Hao Hsu, and Chan-Yen Ou. "CRMP/UNC-33 organizes microtubule bundles for KIF5-mediated mitochondrial distribution to axon." PLOS Genetics 17, no. 2 (February 11, 2021): e1009360. http://dx.doi.org/10.1371/journal.pgen.1009360.

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Neurons are highly specialized cells with polarized cellular processes and subcellular domains. As vital organelles for neuronal functions, mitochondria are distributed by microtubule-based transport systems. Although the essential components of mitochondrial transport including motors and cargo adaptors are identified, it is less clear how mitochondrial distribution among somato-dendritic and axonal compartment is regulated. Here, we systematically study mitochondrial motors, including four kinesins, KIF5, KIF17, KIF1, KLP-6, and dynein, and transport regulators in C. elegans PVD neurons. Among all these motors, we found that mitochondrial export from soma to neurites is mainly mediated by KIF5/UNC-116. Interestingly, UNC-116 is especially important for axonal mitochondria, while dynein removes mitochondria from all plus-end dendrites and the axon. We surprisingly found one mitochondrial transport regulator for minus-end dendritic compartment, TRAK-1, and two mitochondrial transport regulators for axonal compartment, CRMP/UNC-33 and JIP3/UNC-16. While JIP3/UNC-16 suppresses axonal mitochondria, CRMP/UNC-33 is critical for axonal mitochondria; nearly no axonal mitochondria present in unc-33 mutants. We showed that UNC-33 is essential for organizing the population of UNC-116-associated microtubule bundles, which are tracks for mitochondrial trafficking. Disarrangement of these tracks impedes mitochondrial transport to the axon. In summary, we identified a compartment-specific transport regulation of mitochondria by UNC-33 through organizing microtubule tracks for different kinesin motors other than microtubule polarity.
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7

Raynaud, Fabrice, Vincent Homburger, Martial Seveno, Oana Vigy, Enora Moutin, Laurent Fagni, and Julie Perroy. "SNAP23–Kif5 complex controls mGlu1 receptor trafficking." Journal of Molecular Cell Biology 10, no. 5 (September 14, 2018): 423–36. http://dx.doi.org/10.1093/jmcb/mjy031.

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8

Iworima, Diepiriye G., Bryce A. Pasqualotto, and Gordon L. Rintoul. "Kif5 regulates mitochondrial movement, morphology, function and neuronal survival." Molecular and Cellular Neuroscience 72 (April 2016): 22–33. http://dx.doi.org/10.1016/j.mcn.2015.12.014.

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9

Gumy, Laura F., Eugene A. Katrukha, Ilya Grigoriev, Dick Jaarsma, Lukas C. Kapitein, Anna Akhmanova, and Casper C. Hoogenraad. "MAP2 Defines a Pre-axonal Filtering Zone to Regulate KIF1- versus KIF5-Dependent Cargo Transport in Sensory Neurons." Neuron 94, no. 2 (April 2017): 347–62. http://dx.doi.org/10.1016/j.neuron.2017.03.046.

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10

Chen, Yanmin, and Zu-Hang Sheng. "Kinesin-1–syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport." Journal of Cell Biology 202, no. 2 (July 15, 2013): 351–64. http://dx.doi.org/10.1083/jcb.201302040.

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Axonal mitochondria are recruited to synaptic terminals in response to neuronal activity, but the mechanisms underlying activity-dependent regulation of mitochondrial transport are largely unknown. In this paper, using genetic mouse model combined with live imaging, we demonstrate that syntaphilin (SNPH) mediates the activity-dependent immobilization of axonal mitochondria through binding to KIF5. In vitro analysis showed that the KIF5–SNPH coupling inhibited the motor adenosine triphosphatase. Neuronal activity further recruited SNPH to axonal mitochondria. This motor-docking interplay was induced by Ca2+ and synaptic activity and was necessary to establish an appropriate balance between motile and stationary axonal mitochondria. Deleting snph abolished the activity-dependent immobilization of axonal mitochondria. We propose an “Engine-Switch and Brake” model, in which SNPH acts both as an engine off switch by sensing mitochondrial Rho guanosine triphosphatase-Ca2+ and as a brake by anchoring mitochondria to the microtubule track. Altogether, our study provides new mechanistic insight into the molecular interplay between motor and docking proteins, which arrests axonal mitochondrial transport in response to changes in neuronal activity.
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11

Connell, James W., Rachel J. Allison, Catherine E. Rodger, Guy Pearson, Eliska Zlamalova, and Evan Reid. "ESCRT-III-associated proteins and spastin inhibit protrudin-dependent polarised membrane traffic." Cellular and Molecular Life Sciences 77, no. 13 (October 5, 2019): 2641–58. http://dx.doi.org/10.1007/s00018-019-03313-z.

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Abstract Mutations in the gene encoding the microtubule severing ATPase spastin are the most frequent cause of hereditary spastic paraplegia, a genetic condition characterised by length-dependent axonal degeneration. Here, we show that HeLa cells lacking spastin and embryonic fibroblasts from a spastin knock-in mouse model become highly polarised and develop cellular protrusions. In HeLa cells, this phenotype was rescued by wild-type spastin, but not by forms unable to sever microtubules or interact with endosomal ESCRT-III proteins. Cells lacking the spastin-interacting ESCRT-III-associated proteins IST1 or CHMP1B also developed protrusions. The protrusion phenotype required protrudin, a RAB-interacting protein that interacts with spastin and localises to ER–endosome contact sites, where it promotes KIF5-dependent endosomal motility to protrusions. Consistent with this, the protrusion phenotype in cells lacking spastin also required KIF5. Lack or mutation of spastin resulted in functional consequences for receptor traffic of a pathway implicated in HSP, as Bone Morphogenetic Protein receptor distribution became polarised. Our results, therefore, identify a novel role for ESCRT-III proteins and spastin in regulating polarised membrane traffic.
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12

Rahman, Amena, Adeela Kamal, Elizabeth A. Roberts, and Lawrence S. B. Goldstein. "Defective Kinesin Heavy Chain Behavior in Mouse Kinesin Light Chain Mutants." Journal of Cell Biology 146, no. 6 (September 20, 1999): 1277–88. http://dx.doi.org/10.1083/jcb.146.6.1277.

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Conventional kinesin, kinesin-I, is a heterotetramer of two kinesin heavy chain (KHC) subunits (KIF5A, KIF5B, or KIF5C) and two kinesin light chain (KLC) subunits. While KHC contains the motor activity, the role of KLC remains unknown. It has been suggested that KLC is involved in either modulation of KHC activity or in cargo binding. Previously, we characterized KLC genes in mouse (Rahman, A., D.S. Friedman, and L.S. Goldstein. 1998. J. Biol. Chem. 273:15395–15403). Of the two characterized gene products, KLC1 was predominant in neuronal tissues, whereas KLC2 showed a more ubiquitous pattern of expression. To define the in vivo role of KLC, we generated KLC1 gene-targeted mice. Removal of functional KLC1 resulted in significantly smaller mutant mice that also exhibited pronounced motor disabilities. Biochemical analyses demonstrated that KLC1 mutant mice have a pool of KIF5A not associated with any known KLC subunit. Immunofluorescence studies of sensory and motor neuron cell bodies in KLC1 mutants revealed that KIF5A colocalized aberrantly with the peripheral cis-Golgi marker giantin in mutant cells. Striking changes and aberrant colocalization were also observed in the intracellular distribution of KIF5B and β′-COP, a component of COP1 coatomer. Taken together, these data best support models that suggest that KLC1 is essential for proper KHC activation or targeting.
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13

Kanai, Yoshimitsu, Yasushi Okada, Yousuke Tanaka, and Nobutaka Hirokawa. "605 Localization of kinesin heavy chains (KIF5A, KIF5B, KIF5C) in nervous system." Neuroscience Research 28 (January 1997): S84. http://dx.doi.org/10.1016/s0168-0102(97)90217-0.

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14

Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (February 19, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.1.

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Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: The findings raise the possibility that genetic polymorphisms within the KIF5A gene locus could contribute to disturbances of axonal transport, neuronal connectivity and function across a spectrum of neurological conditions, including AD.
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15

Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (June 26, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.2.

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Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: Future in vitro and in vivo studies are required to understand the cause of upregulated KIF5A and KLC-1 gene expression in AD and any potential downstream consequences on pathogenesis, including any contribution of genetic polymorphisms within the KIF5A gene locus.
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16

Schmidt, M. R., T. Maritzen, V. Kukhtina, V. A. Higman, L. Doglio, N. N. Barak, H. Strauss, H. Oschkinat, C. G. Dotti, and V. Haucke. "Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin KIF5 complex." Proceedings of the National Academy of Sciences 106, no. 36 (August 21, 2009): 15344–49. http://dx.doi.org/10.1073/pnas.0904268106.

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17

Rathgeber, Louisa, Kira V. Gromova, Irina Schaefer, Petra Breiden, Christian Lohr, and Matthias Kneussel. "GSK3 and KIF5 regulate activity-dependent sorting of gephyrin between axons and dendrites." European Journal of Cell Biology 94, no. 3-4 (March 2015): 173–78. http://dx.doi.org/10.1016/j.ejcb.2015.01.005.

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18

Takeda, Sen, Hiroto Yamazaki, Dae-Hyun Seog, Yoshimitsu Kanai, Sumio Terada, and Nobutaka Hirokawa. "Kinesin Superfamily Protein 3 (Kif3) Motor Transports Fodrin-Associating Vesicles Important for Neurite Building." Journal of Cell Biology 148, no. 6 (March 20, 2000): 1255–66. http://dx.doi.org/10.1083/jcb.148.6.1255.

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Kinesin superfamily proteins (KIFs) comprise several dozen molecular motor proteins. The KIF3 heterotrimer complex is one of the most abundantly and ubiquitously expressed KIFs in mammalian cells. To unveil the functions of KIF3, microinjection of function-blocking monovalent antibodies against KIF3 into cultured superior cervical ganglion (SCG) neurons was carried out. They significantly blocked fast axonal transport and brought about inhibition of neurite extension. A yeast two-hybrid binding assay revealed the association of fodrin with the KIF3 motor through KAP3. This was further confirmed by using vesicles collected from large bundles of axons (cauda equina), from which membranous vesicles could be prepared in pure preparations. Both immunoprecipitation and immunoelectron microscopy indicated the colocalization of fodrin and KIF3 on the same vesicles, the results reinforcing the evidence that the cargo of the KIF3 motor consists of fodrin-associating vesicles. In addition, pulse-labeling study implied partial comigration of both molecules as fast flow components. Taken together, the KIF3 motor is engaged in fast axonal transport that conveys membranous components important for neurite extension.
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19

Twelvetrees, Alison E., Eunice Y. Yuen, I. Lorena Arancibia-Carcamo, Andrew F. MacAskill, Philippe Rostaing, Michael J. Lumb, Sandrine Humbert, et al. "Delivery of GABAARs to Synapses Is Mediated by HAP1-KIF5 and Disrupted by Mutant Huntingtin." Neuron 65, no. 1 (January 2010): 53–65. http://dx.doi.org/10.1016/j.neuron.2009.12.007.

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20

Cheng, Haixia, Jessica Burroughs-Garcia, Jacqueline E. Birkness, Jonathan C. Trinidad, and Michael R. Deans. "Disparate Regulatory Mechanisms Control Fat3 and P75NTR Protein Transport through a Conserved Kif5-Interaction Domain." PLOS ONE 11, no. 10 (October 27, 2016): e0165519. http://dx.doi.org/10.1371/journal.pone.0165519.

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21

Shi, Ping, Anna-Lena Ström, Jozsef Gal, and Haining Zhu. "Effects of ALS-related SOD1 mutants on dynein- and KIF5-mediated retrograde and anterograde axonal transport." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1802, no. 9 (September 2010): 707–16. http://dx.doi.org/10.1016/j.bbadis.2010.05.008.

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22

Kanai, Yoshimitsu, Yasushi Okada, Yosuke Tanaka, and Nobutaka Hirokawa. "Differential localization of neuronal (KIF5A and KIF 5C) and ubiquitous (KIF5B) kinesin heavy chains in nervous system." Neuroscience Research 31 (January 1998): S132. http://dx.doi.org/10.1016/s0168-0102(98)82022-1.

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23

Noda, Y., R. Sato-Yoshitake, S. Kondo, M. Nangaku, and N. Hirokawa. "KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B." Journal of Cell Biology 129, no. 1 (April 1, 1995): 157–67. http://dx.doi.org/10.1083/jcb.129.1.157.

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Kinesin is known as a representative cytoskeletal motor protein that is engaged in cell division and axonal transport. In addition to the mutant assay, recent advances using the PCR cloning technique have elucidated the existence of many kinds of kinesin-related proteins in yeast, Drosophila, and mice. We previously cloned five different members of kinesin superfamily proteins (KIFs) in mouse brain (Aizawa, H., Y. Sekine, R. Takemura, Z. Zhang, M. Nangaku, and N. Hirokawa. 1992. J. Cell Biol. 119:1287-1296) and demonstrated that one of them, KIF3A, is an anterograde motor (Kondo, S., R. Sato-Yashitake, Y. Noda, H. Aizawa, T. Nakata, Y. Matsuura, and N. Hirokawa. J. Cell Biol. 1994. 125:1095-1107). We have now characterized another axonal transport motor, KIF2. Different from other KIFs, KIF2 is a central type motor, since its motor domain is located in the center of the molecule. Recombinant KIF2 exists as a dimer with a bigger head and plus-end directionally moves microtubules at a velocity of 0.47 +/- 0.11 microns/s, which is two thirds that of kinesin's. Immunocytological examination showed that native KIF2 is abundant in developing axons and that it accumulates in the proximal region of the ligated nerves after a 20-h ligation. Soluble KIF2 exists without a light chain, and KIF2's associated-vesicles, immunoprecipitated by anti-KIF2 antibody, are different from those carried by existing motors such as kinesin and KIF3A. They are also distinct from synaptic vesicles, although KIF2 is accumulated in so-called synaptic vesicle fractions and embryonal growth cone particles. Our results strongly suggest that KIF2 functions as a new anterograde motor, being specialized for a particular group of membranous organelles involved in fast axonal transport.
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Tikhonenko, Irina, Dilip K. Nag, Douglas N. Robinson, and Michael P. Koonce. "Microtubule-Nucleus Interactions in Dictyostelium discoideum Mediated by Central Motor Kinesins." Eukaryotic Cell 8, no. 5 (March 13, 2009): 723–31. http://dx.doi.org/10.1128/ec.00018-09.

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ABSTRACT Kinesins are a diverse superfamily of motor proteins that drive organelles and other microtubule-based movements in eukaryotic cells. These motors play important roles in multiple events during both interphase and cell division. Dictyostelium discoideum contains 13 kinesin motors, 12 of which are grouped into nine families, plus one orphan. Functions for 11 of the 13 motors have been previously investigated; we address here the activities of the two remaining kinesins, both isoforms with central motor domains. Kif6 (of the kinesin-13 family) appears to be essential for cell viability. The partial knockdown of Kif6 with RNA interference generates mitotic defects (lagging chromosomes and aberrant spindle assemblies) that are consistent with kinesin-13 disruptions in other organisms. However, the orphan motor Kif9 participates in a completely novel kinesin activity, one that maintains a connection between the microtubule-organizing center (MTOC) and nucleus during interphase. kif9 null cell growth is impaired, and the MTOC appears to disconnect from its normally tight nuclear linkage. Mitotic spindles elongate in a normal fashion in kif9 − cells, but we hypothesize that this kinesin is important for positioning the MTOC into the nuclear envelope during prophase. This function would be significant for the early steps of cell division and also may play a role in regulating centrosome replication.
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Nakata, Takao, Shinsuke Niwa, Yasushi Okada, Franck Perez, and Nobutaka Hirokawa. "The kinesin-1 motor protein KIF5 recognizes microtubule lattice structure emanated from GTP-tubulin in axons as directional cue." Neuroscience Research 71 (September 2011): e118. http://dx.doi.org/10.1016/j.neures.2011.07.502.

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26

Yue, Yang, T. Lynne Blasius, Stephanie Zhang, Shashank Jariwala, Benjamin Walker, Barry J. Grant, Jared C. Cochran, and Kristen J. Verhey. "Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7." Journal of Cell Biology 217, no. 4 (January 19, 2018): 1319–34. http://dx.doi.org/10.1083/jcb.201708179.

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Kinesin-4 motors play important roles in cell division, microtubule organization, and signaling. Understanding how motors perform their functions requires an understanding of their mechanochemical and motility properties. We demonstrate that KIF27 can influence microtubule dynamics, suggesting a conserved function in microtubule organization across the kinesin-4 family. However, kinesin-4 motors display dramatically different motility characteristics: KIF4 and KIF21 motors are fast and processive, KIF7 and its Drosophila melanogaster homologue Costal2 (Cos2) are immotile, and KIF27 is slow and processive. Neither KIF7 nor KIF27 can cooperate for fast processive transport when working in teams. The mechanistic basis of immotile KIF7 behavior arises from an inability to release adenosine diphosphate in response to microtubule binding, whereas slow processive KIF27 behavior arises from a slow adenosine triphosphatase rate and a high affinity for both adenosine triphosphate and microtubules. We suggest that evolutionarily selected sequence differences enable immotile KIF7 and Cos2 motors to function not as transporters but as microtubule-based tethers of signaling complexes.
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Wu, Zhiqiang, Hao Zhang, Zhengwang Sun, Chunmeng Wang, Yong Chen, Peng Luo, and Wangjun Yan. "Knockdown of Kinesin Family 15 Inhibits Osteosarcoma through Suppressing Cell Proliferation and Promoting Cell Apoptosis." Chemotherapy 64, no. 4 (2019): 187–96. http://dx.doi.org/10.1159/000505014.

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Kinesin family (KIF) members have vital roles in mitosis, meiosis, and transport of macromolecules in eukaryotic cells. In this study, we aimed to investigate the role of KIF15 in osteosarcoma. Immunohistochemical staining was performed to determine expression levels of KIF15 in osteosarcoma tissues and adjacent normal tissues. Tissue microarray analysis showed a correlation between the expression of KIF15 and pathological features of patients. Subsequently, lentivirus was used to inhibit the expression of KIF15 in osteosarcoma cells. An MTT assay was performed to examine cell proliferation. Transwell and wound healing assays were used to estimate the invasion and migration of osteosarcoma cells, respectively. Flow cytometric analysis was employed to define the apoptosis of osteosarcoma cells. Our results showed that KIF15 expression was significantly upregulated in osteosarcoma tissues compared with adjacent normal tissues. The Mann-Whitney U test and Spearman correlation analysis showed that the expression levels of KIF15 in osteosarcoma tissues were positively correlated with tumor infiltrate, a pathological characteristic of patients. The expression of KIF15 was successfully suppressed by shKIF15, and the knockdown efficiency reached 80 and 69% in MNNG/HOS and U2OS cells, respectively. Subsequently, knockdown of KIF15 significantly inhibited the capacity of cell proliferation, colony formation, invasion, and migration, but enhanced G2 phase arrest and partially enhanced cell apoptosis. This study preliminarily showed KIF15 to be a critical regulatory molecule involved in osteosarcoma cell proliferation. Consequently, KIF15 can be a potential diagnostic and therapeutic target for osteosarcoma.
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Sheng, Jiayu, Xiaohong Xue, and Ke Jiang. "Knockdown of Kinase Family 15 Inhibits Cancer Cell Proliferation In vitro and its Clinical Relevance in Triple-Negative Breast Cancer." Current Molecular Medicine 19, no. 2 (May 13, 2019): 147–55. http://dx.doi.org/10.2174/1566524019666190308122108.

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Purpose:Breast cancer is the most prevalent malignancy and the leading cause of death among women. Triple-negative breast cancer (TNBC) is a subtype of breast cancer and shows a distinctly aggressive nature with higher rates of relapse and shorter overall survival in the metastatic setting compared to other subtypes of breast cancer. This study aimed to assess the effect of KIF15 on various clinicopathological characteristics, survival analysis, and cell proliferation in triple-negative breast cancer, which has not been reported to our knowledge.Methods:A total of 165 patients with triple-negative breast cancer were enrolled and clinical data were obtained, Mann-Whitney U analysis was performed to assess the correlation between the expression of KIF15 and clinical pathological characteristics of TNBC patients. Survival analysis was performed by Kaplan-Meier analysis and Log-rank test. The expression levels of KIF15 in cancer tissues and adjacent tissues were evaluated via Sign test. Lentivirus was used to down-regulate the expression of KIF15 in TNBC cells. The cell proliferation, colony formation capacity and apoptosis were examined by MTT, Giemsa staining and flow cytometry assay, respectively.Results:Our results showed that, among the 165 TNBC patients, the expression of KIF15 was positive correlation with clinicopathological features of TNBC. In addition, KIF15 low-expression group showed higher disease-free survival than KIF15 highexpression group and univariate analysis showed that KIF15 high-expression group appeared higher mortality than KIF low-expression group (P ≤ 0.05). Meanwhile, the expression levels of KIF15 in cancer tissue notably up-regulated in comparison with adjacent tissue. In vitro, knockdown of KIF15 significantly promoted cell apoptosis and suppressed cell proliferation and colony formation of TNBC cells.Conclusion:By utilizing survival analysis, we found that high-expression of KIF15 in the TNBC samples were associated with poorer overall survival, while the anti-tumor effect of KIF15 knockdown was also confirmed at the cellular level in vitro. Taken together, KIF15 can be applied as a potential diagnostic and therapeutic target in TNBC.
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Sivaramakrishnan, Sivaraj, Jaime L. Schneider, Albert Sitikov, Robert D. Goldman, and Karen M. Ridge. "Shear Stress Induced Reorganization of the Keratin Intermediate Filament Network Requires Phosphorylation by Protein Kinase C ζ." Molecular Biology of the Cell 20, no. 11 (June 2009): 2755–65. http://dx.doi.org/10.1091/mbc.e08-10-1028.

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Keratin intermediate filaments (KIFs) form a fibrous polymer network that helps epithelial cells withstand external mechanical forces. Recently, we established a correlation between the structure of the KIF network and its local mechanical properties in alveolar epithelial cells. Shear stress applied across the cell surface resulted in the structural remodeling of KIF and a substantial increase in the elastic modulus of the network. This study examines the mechanosignaling that regulates the structural remodeling of the KIF network. We report that the shear stress–mediated remodeling of the KIF network is facilitated by a twofold increase in the dynamic exchange rate of KIF subunits, which is regulated in a PKC ζ and 14-3-3–dependent manner. PKC ζ phosphorylates K18pSer33, and this is required for the structural reorganization because the KIF network in A549 cells transfected with a dominant negative PKC ζ, or expressing the K18Ser33Ala mutation, is unchanged. Blocking the shear stress–mediated reorganization results in reduced cellular viability and increased apoptotic levels. These data suggest that shear stress mediates the phosphorylation of K18pSer33, which is required for the reorganization of the KIF network, resulting in changes in mechanical properties of the cell that help maintain the integrity of alveolar epithelial cells.
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Kumar, Vinod, Jamal-Eddine Bouameur, Janina Bär, Robert H. Rice, Hue-Tran Hornig-Do, Dennis R. Roop, Nicole Schwarz, et al. "A keratin scaffold regulates epidermal barrier formation, mitochondrial lipid composition, and activity." Journal of Cell Biology 211, no. 5 (December 7, 2015): 1057–75. http://dx.doi.org/10.1083/jcb.201404147.

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Keratin intermediate filaments (KIFs) protect the epidermis against mechanical force, support strong adhesion, help barrier formation, and regulate growth. The mechanisms by which type I and II keratins contribute to these functions remain incompletely understood. Here, we report that mice lacking all type I or type II keratins display severe barrier defects and fragile skin, leading to perinatal mortality with full penetrance. Comparative proteomics of cornified envelopes (CEs) from prenatal KtyI−/− and KtyII−/−K8 mice demonstrates that absence of KIF causes dysregulation of many CE constituents, including downregulation of desmoglein 1. Despite persistence of loricrin expression and upregulation of many Nrf2 targets, including CE components Sprr2d and Sprr2h, extensive barrier defects persist, identifying keratins as essential CE scaffolds. Furthermore, we show that KIFs control mitochondrial lipid composition and activity in a cell-intrinsic manner. Therefore, our study explains the complexity of keratinopathies accompanied by barrier disorders by linking keratin scaffolds to mitochondria, adhesion, and CE formation.
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Beech, P. L., K. Pagh-Roehl, Y. Noda, N. Hirokawa, B. Burnside, and J. L. Rosenbaum. "Localization of kinesin superfamily proteins to the connecting cilium of fish photoreceptors." Journal of Cell Science 109, no. 4 (April 1, 1996): 889–97. http://dx.doi.org/10.1242/jcs.109.4.889.

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Kinesin superfamily proteins (KIFs) are probable motors in vesicular and non-vesicular transport along microtubular tracks. Since a variety of KIFs have been recently identified in the motile flagella of Chlamydomonas, we sought to ascertain whether KIFs are also associated with the connecting cilia of vertebrate rod photoreceptors. As the only structural link between the rod inner segment and the photosensitive rod outer segment, the connecting cilium is thought to be the channel through which all material passes into and out of the outer segment from the rod cell body. We have performed immunological tests on isolated sunfish rod inner-outer segments (RIS-ROS) using two antibodies that recognize the conserved motor domain of numerous KIFs (anti-LAGSE, a peptide antibody, and anti-Klp1 head, generated against the N terminus of Chlamydomonas Klp1) as well as an antibody specific to a neuronal KIF, KIF3A. On immunoblots of RIS-ROS, LAGSE antibody detected a prominent band at approximately 117 kDa, which is likely to be kinesin heavy chain, and Klp1 head antibody detected a single band at approximately 170 kDa; KIF3A antibody detected a polypeptide at approximately 85 kDa which co-migrated with mammalian KIF3A and displayed ATP-dependent release from rod cytoskeletons. Immunofluorescence localizations with anti-LAGSE and anti-Klp1 head antibodies detected epitopes in the axoneme and ellipsoid, and immunoelectron microscopy with the LAGSE antibody showed that the connecting cilium region was particularly antigenic. Immunofluorescence with anti-KIF3A showed prominent labelling of the connecting cilium and the area surrounding its basal body; the outer segment axoneme and parts of the inner segment coincident with microtubules were also labelled. We propose that these putative kinesin superfamily proteins may be involved in the translocation of material between the rod inner and outer segments.
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Takeda, Sen, Yoshiaki Yonekawa, Yosuke Tanaka, Yasushi Okada, Shigenori Nonaka, and Nobutaka Hirokawa. "Left-Right Asymmetry and Kinesin Superfamily Protein KIF3A: New Insights in Determination of Laterality and Mesoderm Induction by kif3A−/− Mice Analysis." Journal of Cell Biology 145, no. 4 (May 17, 1999): 825–36. http://dx.doi.org/10.1083/jcb.145.4.825.

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KIF3A is a classical member of the kinesin superfamily proteins (KIFs), ubiquitously expressed although predominantly in neural tissues, and which forms a heterotrimeric KIF3 complex with KIF3B or KIF3C and an associated protein, KAP3. To elucidate the function of the kif3A gene in vivo, we made kif3A knockout mice. kif3A−/− embryos displayed severe developmental abnormalities characterized by neural tube degeneration and mesodermal and caudal dysgenesis and died during the midgestational period at ∼10.5 dpc (days post coitum), possibly resulting from cardiovascular insufficiency. Whole mount in situ hybridization of Pax6 revealed a normal pattern while staining by sonic hedgehog (shh) and Brachyury (T) exhibited abnormal patterns in the anterior-posterior (A-P) direction at both mesencephalic and thoracic levels. These results suggest that KIF3A might be involved in mesodermal patterning and in turn neurogenesis.
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Gache, V., E. R. Gomes, and B. Cadot. "Microtubule motors involved in nuclear movement during skeletal muscle differentiation." Molecular Biology of the Cell 28, no. 7 (April 2017): 865–74. http://dx.doi.org/10.1091/mbc.e16-06-0405.

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Nuclear positioning is a determining event in several cellular processes, such as fertilization, cell migration, and cell differentiation. The structure and function of muscle cells, which contain hundreds of nuclei, have been shown to rely in part on proper nuclear positioning. Remarkably, in the course of muscle differentiation, nuclear movements along the myotube axis might represent the event required for the even positioning of nuclei in the mature myofiber. Here we analyze nuclear behavior, time in motion, speed, and alignment during myotube differentiation and temporal interference of cytoskeletal microtubule-related motors. Using specific inhibitors, we find that nuclear movement and alignment are microtubule dependent, with 19 microtubule motor proteins implicated in at least one nuclear behavior. We further focus on Kif1c, Kif5b, kif9, kif21b, and Kif1a, which affect nuclear alignment. These results emphasize the different roles of molecular motors in particular mechanisms.
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Mahase, Vidhyanand, Adebiyi Sobitan, Christina Johnson, Farion Cooper, Yixin Xie, Lin Li, and Shaolei Teng. "Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A." Journal of Theoretical and Computational Chemistry 19, no. 06 (August 5, 2020): 2041003. http://dx.doi.org/10.1142/s0219633620410035.

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Hereditary spastic paraplegias (HSPs) are a genetically heterogeneous collection of neurodegenerative disorders categorized by progressive lower-limb spasticity and frailty. The complex HSP forms are characterized by various neurological features including progressive spastic weakness, urinary sphincter dysfunction, extra pyramidal signs and intellectual disability (ID). The kinesin superfamily proteins (KIFs) are microtubule-dependent molecular motors involved in intracellular transport. Kinesins directionally transport membrane vesicles, protein complexes, and mRNAs along neurites, thus playing important roles in neuronal development and function. Recent genetic studies have identified kinesin mutations in patients with HSPs. In this study, we used the computational approaches to investigate the 40 missense mutations associated with HSP and ID in KIF1A and KIF5A. We performed homology modeling to construct the structures of kinesin–microtubule binding domain and kinesin–tubulin complex. We applied structure-based energy calculation methods to determine the effects of missense mutations on protein stability and protein–protein interaction. The results revealed that the most of disease-causing mutations could change the folding free energy of kinesin motor domain and the binding free energy of kinesin–tubulin complex. We found that E253K associated with ID in KIF1A decrease the protein stability of kinesin motor domains. We showed that the HSP mutations located in kinesin–tubulin complex interface, such as K253N and R280C in KIF5A, can destabilize the kinesin–tubulin complex. The computational analysis provides useful information for understanding the roles of kinesin mutations in the development of ID and HSPs.
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Cho, Kyoung‐in, Yunfei Cai, Haiqing Yi, Andrew Yeh, Azamat Aslanukov, and Paulo A. Ferreira. "Association of the Kinesin‐Binding Domain of RanBP2 to KIF5B and KIF5C Determines Mitochondria Localization and Function." Traffic 8, no. 12 (August 30, 2007): 1722–35. http://dx.doi.org/10.1111/j.1600-0854.2007.00647.x.

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36

McHugh, Toni, Hauke Drechsler, Andrew D. McAinsh, Nicolas J. Carter, and Robert A. Cross. "Kif15 functions as an active mechanical ratchet." Molecular Biology of the Cell 29, no. 14 (July 15, 2018): 1743–52. http://dx.doi.org/10.1091/mbc.e18-03-0151.

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Kif15 is a kinesin-12 that contributes critically to bipolar spindle assembly in humans. Here we use force-ramp experiments in an optical trap to probe the mechanics of single Kif15 molecules under hindering or assisting loads and in a variety of nucleotide states. While unloaded Kif15 is established to be highly processive, we find that under hindering loads, Kif15 takes <∼10 steps. As hindering load is increased, Kif15 forestep:backstep ratio decreases exponentially, with stall occurring at 6 pN. In contrast, under assisting loads, Kif15 detaches readily and rapidly, even from its AMPPNP state. Kif15 mechanics thus depend markedly on the loading direction. Kif15 interacts with a binding partner, Tpx2, and we show that Tpx2 locks Kif15 to microtubules under both hindering and assisting loads. Overall, our data predict that Kif15 in the central spindle will act as a mechanical ratchet, supporting spindle extension but resisting spindle compression.
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Milic, Bojan, Anirban Chakraborty, Kyuho Han, Michael C. Bassik, and Steven M. Block. "KIF15 nanomechanics and kinesin inhibitors, with implications for cancer chemotherapeutics." Proceedings of the National Academy of Sciences 115, no. 20 (April 27, 2018): E4613—E4622. http://dx.doi.org/10.1073/pnas.1801242115.

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Eg5, a mitotic kinesin, has been a target for anticancer drug development. Clinical trials of small-molecule inhibitors of Eg5 have been stymied by the development of resistance, attributable to mitotic rescue by a different endogenous kinesin, KIF15. Compared with Eg5, relatively little is known about the properties of the KIF15 motor. Here, we employed single-molecule optical-trapping techniques to define the KIF15 mechanochemical cycle. We also studied the inhibitory effects of KIF15-IN-1, an uncharacterized, commercially available, small-molecule inhibitor, on KIF15 motility. To explore the complementary behaviors of KIF15 and Eg5, we also scored the effects of small-molecule inhibitors on admixtures of both motors, using both a microtubule (MT)-gliding assay and an assay for cancer cell viability. We found that (i) KIF15 motility differs significantly from Eg5; (ii) KIF15-IN-1 is a potent inhibitor of KIF15 motility; (iii) MT gliding powered by KIF15 and Eg5 only ceases when both motors are inhibited; and (iv) pairing KIF15-IN-1 with Eg5 inhibitors synergistically reduces cancer cell growth. Taken together, our results lend support to the notion that a combination drug therapy employing both inhibitors may be a viable strategy for overcoming chemotherapeutic resistance.
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Mann, Barbara J., Sai K. Balchand, and Patricia Wadsworth. "Regulation of Kif15 localization and motility by the C-terminus of TPX2 and microtubule dynamics." Molecular Biology of the Cell 28, no. 1 (January 2017): 65–75. http://dx.doi.org/10.1091/mbc.e16-06-0476.

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Mitotic motor proteins generate force to establish and maintain spindle bipolarity, but how they are temporally and spatially regulated in vivo is unclear. Prior work demonstrated that a microtubule-associated protein, TPX2, targets kinesin-5 and kinesin-12 motors to spindle microtubules. The C-terminal domain of TPX2 contributes to the localization and motility of the kinesin-5, Eg5, but it is not known whether this domain regulates kinesin-12, Kif15. We found that the C-terminal domain of TPX2 contributes to the localization of Kif15 to spindle microtubules in cells and suppresses motor walking in vitro. Kif15 and Eg5 are partially redundant motors, and overexpressed Kif15 can drive spindle formation in the absence of Eg5 activity. Kif15-dependent bipolar spindle formation in vivo requires the C-terminal domain of TPX2. In the spindle, fluorescent puncta of GFP-Kif15 move toward the equatorial region at a rate equivalent to microtubule growth. Reduction of microtubule growth with paclitaxel suppresses GFP-Kif15 motility, demonstrating that dynamic microtubules contribute to Kif15 behavior. Our results show that the C-terminal region of TPX2 regulates Kif15 in vitro, contributes to motor localization in cells, and is required for Kif15 force generation in vivo and further reveal that dynamic microtubules contribute to Kif15 behavior in vivo.
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Cai, Yunfei, Brij B. Singh, Azamat Aslanukov, Haiyan Zhao, and Paulo A. Ferreira. "The Docking of Kinesins, KIF5B and KIF5C, to Ran-binding Protein 2 (RanBP2) Is Mediated via a Novel RanBP2 Domain." Journal of Biological Chemistry 276, no. 45 (September 11, 2001): 41594–602. http://dx.doi.org/10.1074/jbc.m104514200.

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40

Tian, Da-Wei, Zhou-Liang Wu, Li-Ming Jiang, Jie Gao, Chang-Li Wu, and Hai-Long Hu. "KIF5A Promotes Bladder Cancer Proliferation In Vitro and In Vivo." Disease Markers 2019 (July 3, 2019): 1–9. http://dx.doi.org/10.1155/2019/4824902.

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Background. Bladder cancer is a common malignancy with uncontrolled and rapid growth. Although lots of the important regulatory networks in bladder cancer have been found, the cancer-relevant genes remain to be further identified. Methods. We examined the KIF5A expression levels in bladder cancer and normal bladder tissue samples via immunohistochemistry and observed the effect of KIF5A on bladder tumor cell proliferation in vitro and in vivo. Additionally, a coexpression between KIF5A and KIF20B in tumor tissues was explored. Results. KIF5A expression level was higher in the bladder cancer tissues than in the adjacent nontumor tissues. Patients with higher KIF5A expression displayed advanced clinical features and shorter survival time than those with lower KIF5A expression. Moreover, KIF5A knockdown inhibited bladder cancer cell proliferation, migration, and invasion demonstrated in vivo and in vitro. In addition, coexpression was found between KIF5A and KIF20B in tumor tissues. Conclusion. The results demonstrated that KIF5A is a critical regulator in bladder cancer development and progression, as well as a potential target in the treatment of bladder cancer.
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41

Kanamarlapudi, V. "Centaurin-α1 and KIF13B kinesin motor protein interaction in ARF6 signalling." Biochemical Society Transactions 33, no. 6 (October 26, 2005): 1279–81. http://dx.doi.org/10.1042/bst0331279.

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The ARF (ADP-ribosylation factor) family of small GTPases regulate intracellular membrane trafficking by cycling between an inactive GDP- and an active GTP-bound form. Among the six known mammalian ARFs (ARF1–ARF6), ARF6 is the least conserved and plays critical roles in membrane trafficking and cytoskeletal dynamics near the cell surface. Since ARFs have undetectable levels of intrinsic GTP binding and hydrolysis, they are totally dependent on extrinsic GEFs (guanine nucleotide-exchange factors) for GTP binding and GAPs (GTPase-activating proteins) for GTP hydrolysis. We have recently isolated a novel KIF (kinesin) motor protein (KIF13B) that binds to centaurin-α1, an ARF6GAP that binds to the second messenger PIP3 [PtdIns(3,4,5)P3]. KIFs transport intracellular vesicles and recognize their cargo by binding to proteins (receptors) localized on the surface of the cargo vesicles. Identification of centaurin-α1 as a KIF13B interactor suggests that KIF13B may transport ARF6 and/or PIP3 using centaurin-α1 as its receptor. This paper reviews the studies carried out to assess the interaction and regulation of centaurin-α1 by KIF13B.
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42

Pozo, K., and F. A. Stephenson. "GRIF-1–kinesin-1 interactions: a confocal microscopy study." Biochemical Society Transactions 34, no. 1 (January 20, 2006): 48–50. http://dx.doi.org/10.1042/bst0340048.

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GRIF-1 [GABAA (γ-aminobutyric acidA) receptor interacting factor-1] is a member of a coiled-coil family of proteins thought to function as adaptors in the anterograde trafficking of organelles utilizing the kinesin-1 motor proteins to synapses. To study in more detail the molecular interaction between GRIF-1 and the kinesin-1 family member KIF5C, fluorescent yellow- and fluorescent cyan-tagged GRIF-1, KIF5C, the KIF5C MD (motor domain) and the KIF5C NMD (non-motor domain) fusion proteins were generated. Each was characterized with respect to size and ability to co-associate by immunoprecipitation following expression in HEK-293 (human embryonic kidney 293) cells. Further, their distribution in transfected HEK-293 and transformed African green monkey kidney (COS-7) cells was analysed by confocal microscopy. The fluorescent GRIF-1 and KIF5C fusion proteins were all found to behave as wild-type. Double GRIF-1/KIF5C transfectants revealed co-localization. The GRIF-1/KIF5C and GRIF-1/KIF5C NMD double transfectants showed different subcellular distributions compared with single GRIF-1, KIF5C or KIF5C NMD transfections. These studies confirm the association between GRIF-1 and kinesin-1 NMDs. Fluorescence resonance energy transfer studies are ongoing to characterize this interaction in more detail.
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43

LEE, Young M., Seungoh LEE, Eunyoung LEE, Hyunjin SHIN, Hwasun HAHN, Wonja CHOI, and Wankee KIM. "Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis." Biochemical Journal 360, no. 3 (December 10, 2001): 549–56. http://dx.doi.org/10.1042/bj3600549.

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In a previous study, we identified the human counterpart of murine kinesin superfamily member 4 (KIF4), a microtubule-based motor protein [Oh, Hahn, Torrey, Shin, Choi, Lee, Morse and Kim (2000) Biochim. Biophys. Acta 1493, 219–224]. As an initial step to understand the function(s) of human KIF4, its subcellular localization in HeLa cells was examined by using immunocytochemical and subcellular fractionation methods, and it was found that most KIF4 is localized in the nucleus. Since murine KIF4 is known to transport cytoplasmic vesicles, dominant nuclear localization of the human counterpart was somewhat surprising. Subsequent subnuclear fractionation revealed predominant association of KIF4 with the nuclear matrix. These results clearly indicate that human KIF4 is, at least, a nuclear protein. In further confirmation of this conclusion, the hexapeptide PKLRRR (amino acids 773–778) in the molecule was found to function as a nuclear localization signal. During the mitotic phase of the cell cycle, human KIF4 was associated with the chromosomes, suggesting that human KIF4 might be a microtubule-based mitotic motor, with DNA as its cargo.
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Qiao, Yuan, Jingtao Chen, Chao Ma, Yingmin Liu, Peitong Li, Yalin Wang, Lin Hou, and Ziling Liu. "Increased KIF15 Expression Predicts a Poor Prognosis in Patients with Lung Adenocarcinoma." Cellular Physiology and Biochemistry 51, no. 1 (2018): 1–10. http://dx.doi.org/10.1159/000495155.

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Background/Aims: Lung cancer is the leading cause of cancer-related deaths worldwide. The outcome of patients with non-small cell lung cancer remains poor; the 5-year survival rate for stage IV non-small cell lung cancer is only 1.0%. KIF15 is a tetrameric kinesin spindle motor that has been investigated for its regulation of mitosis. While the roles of kinesin motor proteins in the regulation of mitosis and their potentials as therapeutic targets in pancreatic cancer have been described previously, the role of KIF15 in lung cancer development remains unknown. Methods: Paired lung carcinoma specimens and matched adjacent normal tissues were used for protein analysis. Clinical data were obtained from medical records. We first examined KIF15 messenger RNA expression in The Cancer Genome Atlas database, and then determined KIF15 protein levels using immunohistochemistry and western blotting. Differences between the groups were analyzed using repeated measures analysis of variance. Overall survival was analyzed using the Kaplan–Meier method. Cell-cycle and proliferation assays were conducted using A549, NCI-H1299, and NCI-H226 cells. Results: KIF15 was significantly upregulated at both the messenger RNA and protein levels in human lung tumor tissues. In patients with lung adenocarcinoma, KIF15 expression was positively associated with disease stages; high KIF15 expression predicted a poor prognosis. KIF15 knockdown using short hairpin RNA in two human lung adenocarcinoma cell lines induced G1/S phase cell cycle arrest and inhibited cell growth, but there was no effect in human lung squamous cell carcinoma. Conclusion: Our findings show that KIF15 is involved in lung cancer carcinogenesis. KIF15 could therefore serve as a specific prognostic marker for patients with lung adenocarcinoma.
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45

Sekine, Y., Y. Okada, Y. Noda, S. Kondo, H. Aizawa, R. Takemura, and N. Hirokawa. "A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally." Journal of Cell Biology 127, no. 1 (October 1, 1994): 187–201. http://dx.doi.org/10.1083/jcb.127.1.187.

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To understand the mechanisms of transport for organelles in the axon, we isolated and sequenced the cDNA encoding KIF4 from murine brain, and characterized the molecule biochemically and immunocytochemically. Complete amino acid sequence analysis of KIF4 and ultrastructural studies of KIF4 molecules expressed in Sf9 cells revealed that the protein contains 1,231 amino acid residues (M(r) 139,550) and that the molecule (116-nm rod with globular heads and tail) consists of three domains: an NH2-terminal globular motor domain, a central alpha-helical stalk domain and a COOH-terminal tail domain. KIF4 protein has the property of nucleotide-dependent binding to microtubules, microtubule-activated ATPase activity, and microtubule plus-end-directed motility. Northern blot analysis and in situ hybridization demonstrated that KIF4 is strongly expressed in juvenile tissues including differentiated young neurons, while its expression is decreased considerably in adult mice except in spleen. Immunocytochemical studies revealed that KIF4 colocalized with membranous organelles both in growth cones of differentiated neurons and in the cytoplasm of cultured fibroblasts. During mitotic phase of cell cycle, KIF4 appears to colocalize with membranous organelles in the mitotic spindle. Hence we conclude that KIF4 is a novel microtubule-associated anterograde motor protein for membranous organelles, the expression of which is regulated developmentally.
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Sun, Yue-Feng, Hong-Li Wu, Rui-Fang Shi, Lin Chen, and Chao Meng. "KIF15 Promotes Proliferation and Growth of Hepatocellular Carcinoma." Analytical Cellular Pathology 2020 (April 3, 2020): 1–9. http://dx.doi.org/10.1155/2020/6403012.

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Liver cancer is thought as the most common human malignancy worldwide, and hepatocellular carcinoma (HCC) accounts for nearly 90% liver cancer. Due to its poor early diagnosis and limited treatment, HCC has therefore become the most lethal malignant cancers in the world. Recently, molecular targeted therapies showed great promise in the treatment of HCC, and novel molecular therapeutic targets is urgently needed. KIF15 is a microtubule-dependent motor protein involved in multiple cell processes, such as cell division. Additionally, KIF15 has been reported to participate in the growth of various types of tumors; however, the relation between KIF15 and HCC is unclear. Herein, our study investigated the possible role of KIF15 on the progression of HCC and found that KIF15 has high expression in tumor samples from HCC patients. KIF15 could play a critical role in the regulation of cell proliferation of HCC, which was proved by in vitro and in vivo assays. In conclusion, this study confirmed that KIF15 could be a novel therapeutic target for the treatment of HCC.
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47

Heath, Carissa M., and Sarah M. Wignall. "Chromokinesin Kif4 promotes proper anaphase in mouse oocyte meiosis." Molecular Biology of the Cell 30, no. 14 (July 2019): 1691–704. http://dx.doi.org/10.1091/mbc.e18-10-0666.

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Oocytes of many species lack centrioles and therefore form acentriolar spindles. Despite the necessity of oocyte meiosis for successful reproduction, how these spindles mediate accurate chromosome segregation is poorly understood. We have gained insight into this process through studies of the kinesin-4 family member Kif4 in mouse oocytes. We found that Kif4 localizes to chromosomes through metaphase and then largely redistributes to the spindle midzone during anaphase, transitioning from stretches along microtubules to distinct ring-like structures; these structures then appear to fuse together by telophase. Kif4’s binding partner PRC1 and MgcRacGAP, a component of the centralspindlin complex, have a similar localization pattern, demonstrating dynamic spindle midzone organization in oocytes. Kif4 knockdown results in defective midzone formation and longer spindles, revealing new anaphase roles for Kif4 in mouse oocytes. Moreover, inhibition of Aurora B/C kinases results in Kif4 mislocalization and causes anaphase defects. Taken together, our work reveals essential roles for Kif4 during the meiotic divisions, furthering our understanding of mechanisms promoting accurate chromosome segregation in acentriolar oocytes.
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Peretti, Diego, Leticia Peris, Silvana Rosso, Santiago Quiroga, and Alfredo Cáceres. "Evidence for the Involvement of Kif4 in the Anterograde Transport of L1-Containing Vesicles." Journal of Cell Biology 149, no. 1 (April 3, 2000): 141–52. http://dx.doi.org/10.1083/jcb.149.1.141.

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In this study we present evidence about the cellular functions of KIF4. Using subcellular fractionation techniques and immunoisolation, we have now identified a type of vesicle that associates with KIF4, an NH2-terminal globular motor domain kinesin-like protein. This vesicle is highly concentrated in growth cones and contains L1, a cell adhesion molecule implicated in axonal elongation. It lacks synaptic vesicle markers, receptors for neurotrophins, and membrane proteins involved in growth cone guidance. In cultured neurons, KIF4 and L1 predominantly localize to the axonal shaft and its growth cone. Suppression of KIF4 with antisense oligonucleotides results in the accumulation of L1 within the cell body and in its complete disappearance from axonal tips. In addition, KIF4 suppression prevents L1-enhanced axonal elongation. Taken collectively, our results suggest an important role for KIF4 during neuronal development, a phenomenon which may be related to the anterograde transport of L1-containing vesicles.
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49

Yi, Peng, Li Li Chew, Ziwang Zhang, Hao Ren, Feiya Wang, Xiaoxia Cong, Liling Zheng, et al. "KIF5B transports BNIP-2 to regulate p38 mitogen-activated protein kinase activation and myoblast differentiation." Molecular Biology of the Cell 26, no. 1 (January 2015): 29–42. http://dx.doi.org/10.1091/mbc.e14-03-0797.

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The Cdo-p38MAPK (p38 mitogen-activated protein kinase) signaling pathway plays important roles in regulating skeletal myogenesis. During myogenic differentiation, the cell surface receptor Cdo bridges scaffold proteins BNIP-2 and JLP and activates p38MAPK, but the spatial-temporal regulation of this process is largely unknown. We here report that KIF5B, the heavy chain of kinesin-1 motor, is a novel interacting partner of BNIP-2. Coimmunoprecipitation and far-Western study revealed that BNIP-2 directly interacted with the motor and tail domains of KIF5B via its BCH domain. By using a range of organelle markers and live microscopy, we determined the endosomal localization of BNIP-2 and revealed the microtubule-dependent anterograde transport of BNIP-2 in C2C12 cells. The anterograde transport of BNIP-2 was disrupted by a dominant-negative mutant of KIF5B. In addition, knockdown of KIF5B causes aberrant aggregation of BNIP-2, confirming that KIF5B is critical for the anterograde transport of BNIP-2 in cells. Gain- and loss-of-function experiments further showed that KIF5B modulates p38MAPK activity and in turn promotes myogenic differentiation. Of importance, the KIF5B-dependent anterograde transport of BNIP-2 is critical for its promyogenic effects. Our data reveal a novel role of KIF5B in the spatial regulation of Cdo–BNIP-2–p38MAPK signaling and disclose a previously unappreciated linkage between the intracellular transporting system and myogenesis regulation.
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50

Malaby, Heidi L. H., Megan E. Dumas, Ryoma Ohi, and Jason Stumpff. "Kinesin-binding protein ensures accurate chromosome segregation by buffering KIF18A and KIF15." Journal of Cell Biology 218, no. 4 (February 1, 2019): 1218–34. http://dx.doi.org/10.1083/jcb.201806195.

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Mitotic kinesins must be regulated to ensure a precise balance of spindle forces and accurate segregation of chromosomes into daughter cells. Here, we demonstrate that kinesin-binding protein (KBP) reduces the activity of KIF18A and KIF15 during metaphase. Overexpression of KBP disrupts the movement and alignment of mitotic chromosomes and decreases spindle length, a combination of phenotypes observed in cells deficient for KIF18A and KIF15, respectively. We show through gliding filament and microtubule co-pelleting assays that KBP directly inhibits KIF18A and KIF15 motor activity by preventing microtubule binding. Consistent with these effects, the mitotic localizations of KIF18A and KIF15 are altered by overexpression of KBP. Cells depleted of KBP exhibit lagging chromosomes in anaphase, an effect that is recapitulated by KIF15 and KIF18A overexpression. Based on these data, we propose a model in which KBP acts as a protein buffer in mitosis, protecting cells from excessive KIF18A and KIF15 activity to promote accurate chromosome segregation.
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