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Journal articles on the topic 'Retrograde protein 1'

Author: Grafiati
Published: 6 September 2023

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1

Blacque, Oliver E., Chunmei Li, Peter N. Inglis, et al. "The WD Repeat-containing Protein IFTA-1 Is Required for Retrograde Intraflagellar Transport." Molecular Biology of the Cell 17, no. 12 (2006): 5053–62. http://dx.doi.org/10.1091/mbc.e06-06-0571.

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The assembly and maintenance of cilia require intraflagellar transport (IFT), a microtubule-dependent bidirectional motility of multisubunit protein complexes along ciliary axonemes. Defects in IFT and the functions of motile or sensory cilia are associated with numerous human ailments, including polycystic kidney disease and Bardet–Biedl syndrome. Here, we identify a novel Caenorhabditis elegans IFT gene, IFT-associated gene 1 (ifta-1), which encodes a WD repeat-containing protein with strong homology to a mammalian protein of unknown function. Both the C. elegans and human IFTA-1 proteins lo
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2

Schafer, Jenny C., Courtney J. Haycraft, James H. Thomas, Bradley K. Yoder, and Peter Swoboda. "XBX-1 Encodes a Dynein Light Intermediate Chain Required for Retrograde Intraflagellar Transport and Cilia Assembly in Caenorhabditis elegans." Molecular Biology of the Cell 14, no. 5 (2003): 2057–70. http://dx.doi.org/10.1091/mbc.e02-10-0677.

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Intraflagellar transport (IFT) is a process required for flagella and cilia assembly that describes the dynein and kinesin mediated movement of particles along axonemes that consists of an A and a B complex, defects in which disrupt retrograde and anterograde transport, respectively. Herein, we describe a novel Caenorhabditis elegans gene, xbx-1, that is required for retrograde IFT and shares homology with a mammalian dynein light intermediate chain (D2LIC). xbx-1 expression in ciliated sensory neurons is regulated by the transcription factor DAF-19, as demonstrated previously for genes encodi
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3

Anderson, Nadine S., Indrani Mukherjee, Christine M. Bentivoglio, and Charles Barlowe. "The golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs." Molecular Biology of the Cell 28, no. 20 (2017): 2686–700. http://dx.doi.org/10.1091/mbc.e17-03-0137.

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Extended coiled-coil proteins of the golgin family play prominent roles in maintaining the structure and function of the Golgi complex. Here we further investigate the golgin protein Coy1 and document its function in retrograde transport between early Golgi compartments. Cells that lack Coy1 displayed a reduced half-life of the Och1 mannosyltransferase, an established cargo of intra-Golgi retrograde transport. Combining the coy1Δ mutation with deletions in other putative retrograde golgins (sgm1Δ and rud3Δ) caused strong glycosylation and growth defects and reduced membrane association of the
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4

Hollenbeck, P. J., and D. Bray. "Rapidly transported organelles containing membrane and cytoskeletal components: their relation to axonal growth." Journal of Cell Biology 105, no. 6 (1987): 2827–35. http://dx.doi.org/10.1083/jcb.105.6.2827.

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We have examined the movements, composition, and cellular origin of phase-dense varicosities in cultures of chick sympathetic and sensory neurons. These organelles are variable in diameter (typically between 0.2 and 2 microns) and undergo saltatory movements both towards and away from the neuronal cell body. Their mean velocities vary inversely with the size of the organelle and are greater in the retrograde than the anterograde direction. Organelles stain with the lipophilic dye 1, 1'-dioctadecyl-3,3,3',3'-tetramethyl-indocarbocyanine and with antibodies to cytoskeletal components. In culture
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5

Buser, Dominik P., Kai D. Schleicher, Cristina Prescianotto-Baschong, and Martin Spiess. "A versatile nanobody-based toolkit to analyze retrograde transport from the cell surface." Proceedings of the National Academy of Sciences 115, no. 27 (2018): E6227—E6236. http://dx.doi.org/10.1073/pnas.1801865115.

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Retrograde transport of membranes and proteins from the cell surface to the Golgi and beyond is essential to maintain homeostasis, compartment identity, and physiological functions. To study retrograde traffic biochemically, by live-cell imaging or by electron microscopy, we engineered functionalized anti-GFP nanobodies (camelid VHH antibody domains) to be bacterially expressed and purified. Tyrosine sulfation consensus sequences were fused to the nanobody for biochemical detection of trans-Golgi arrival, fluorophores for fluorescence microscopy and live imaging, and APEX2 (ascorbate peroxidas
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6

Shimizu, Takayuki, Sylwia M. Kacprzak, Nobuyoshi Mochizuki, et al. "The retrograde signaling protein GUN1 regulates tetrapyrrole biosynthesis." Proceedings of the National Academy of Sciences 116, no. 49 (2019): 24900–24906. http://dx.doi.org/10.1073/pnas.1911251116.

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The biogenesis of the photosynthetic apparatus in developing seedlings requires the assembly of proteins encoded on both nuclear and chloroplast genomes. To coordinate this process there needs to be communication between these organelles, but the retrograde signals by which the chloroplast communicates with the nucleus at this time are still essentially unknown. The Arabidopsis thaliana genomes uncoupled (gun) mutants, that show elevated nuclear gene expression after chloroplast damage, have formed the basis of our understanding of retrograde signaling. Of the 6 reported gun mutations, 5 are i
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7

Signor, Dawn, Karen P. Wedaman, Jose T. Orozco, et al. "Role of a Class Dhc1b Dynein in Retrograde Transport of Ift Motors and Ift Raft Particles along Cilia, but Not Dendrites, in Chemosensory Neurons of Living Caenorhabditis elegans." Journal of Cell Biology 147, no. 3 (1999): 519–30. http://dx.doi.org/10.1083/jcb.147.3.519.

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The heterotrimeric motor protein, kinesin-II, and its presumptive cargo, can be observed moving anterogradely at 0.7 μm/s by intraflagellar transport (IFT) within sensory cilia of chemosensory neurons of living Caenorhabditis elegans, using a fluorescence microscope–based transport assay (Orozco, J.T., K.P. Wedaman, D. Signor, H. Brown, L. Rose, and J.M. Scholey. 1999. Nature. 398:674). Here, we report that kinesin-II, and two of its presumptive cargo molecules, OSM-1 and OSM-6, all move at ∼1.1 μm/s in the retrograde direction along cilia and dendrites, which is consistent with the hypothesis
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8

Cavolo, Samantha L., Chaoming Zhou, Stephanie A. Ketcham, et al. "Mycalolide B dissociates dynactin and abolishes retrograde axonal transport of dense-core vesicles." Molecular Biology of the Cell 26, no. 14 (2015): 2664–72. http://dx.doi.org/10.1091/mbc.e14-11-1564.

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Axonal transport is critical for maintaining synaptic transmission. Of interest, anterograde and retrograde axonal transport appear to be interdependent, as perturbing one directional motor often impairs movement in the opposite direction. Here live imaging of Drosophila and hippocampal neuron dense-core vesicles (DCVs) containing a neuropeptide or brain-derived neurotrophic factor shows that the F-actin depolymerizing macrolide toxin mycalolide B (MB) rapidly and selectively abolishes retrograde, but not anterograde, transport in the axon and the nerve terminal. Latrunculin A does not mimic M
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9

Ramos-García, Silvia L., Robert W. Roberson, Michael Freitag, Salomón Bartnicki-García, and Rosa R. Mouriño-Pérez. "Cytoplasmic Bulk Flow Propels Nuclei in Mature Hyphae of Neurospora crassa." Eukaryotic Cell 8, no. 12 (2009): 1880–90. http://dx.doi.org/10.1128/ec.00062-09.

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ABSTRACT We used confocal microscopy to evaluate nuclear dynamics in mature, growing hyphae of Neurospora crassa whose nuclei expressed histone H1-tagged green fluorescent protein (GFP). In addition to the H1-GFP wild-type (WT) strain, we examined nuclear displacement (passive transport) in four mutants deficient in microtubule-related motor proteins (ro-1, ro-3, kin-1, and a ro-1 kin-1 double mutant). We also treated the WT strain with benomyl and cytochalasin A to disrupt microtubules and actin microfilaments, respectively. We found that the degree of nuclear displacement in the subapical re
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Giannotta, Monica, Giorgia Fragassi, Antonio Tamburro, Capone Vanessa, Alberto Luini, and Michele Sallese. "Prohibitin: A Novel Molecular Player in KDEL Receptor Signalling." BioMed Research International 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/319454.

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The KDEL receptor (KDELR) is a seven-transmembrane-domain protein involved in retrograde transport of protein chaperones from the Golgi complex to the endoplasmic reticulum. Our recent findings have shown that the Golgi-localised KDELR acts as a functional G-protein-coupled receptor by binding to and activating Gs and Gq. These G proteins induce activation of PKA and Src and regulate retrograde and anterograde Golgi trafficking. Here we used an integrated coimmunoprecipitation and mass spectrometry approach to identify prohibitin-1 (PHB) as a KDELR interactor. PHB is a multifunctional protein
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11

Holifield, B. F., A. Ishihara, and K. Jacobson. "Comparative behavior of membrane protein-antibody complexes on motile fibroblasts: implications for a mechanism of capping." Journal of Cell Biology 111, no. 6 (1990): 2499–512. http://dx.doi.org/10.1083/jcb.111.6.2499.

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A characteristic feature of fibroblast locomotory activity is the rearward transport across the leading lamella of various materials used to mark the cell surface. The two processes most frequently invoked as explanations for this transport phenomenon, called capping, are (a) retrograde membrane flow arising from directed membrane insertion and (b) rearward cortical cytoskeletal flow arising from cytoskeletal assembly and contraction. The retrograde lipid flow hypothesis, the most current form of the membrane flow scheme, makes explicit predictions about the movement of membrane proteins subje
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12

Marx, Astrid, William J. Godinez, Vasil Tsimashchuk, Peter Bankhead, Karl Rohr, and Ulrike Engel. "Xenopus cytoplasmic linker–associated protein 1 (XCLASP1) promotes axon elongation and advance of pioneer microtubules." Molecular Biology of the Cell 24, no. 10 (2013): 1544–58. http://dx.doi.org/10.1091/mbc.e12-08-0573.

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Dynamic microtubules (MTs) are required for neuronal guidance, in which axons extend directionally toward their target tissues. We found that depletion of the MT-binding protein Xenopus cytoplasmic linker–associated protein 1 (XCLASP1) or treatment with the MT drug Taxol reduced axon outgrowth in spinal cord neurons. To quantify the dynamic distribution of MTs in axons, we developed an automated algorithm to detect and track MT plus ends that have been fluorescently labeled by end-binding protein 3 (EB3). XCLASP1 depletion reduced MT advance rates in neuronal growth cones, very much like treat
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13

Jovasevic, Vladimir, Mojgan H. Naghavi, and Derek Walsh. "Microtubule plus end–associated CLIP-170 initiates HSV-1 retrograde transport in primary human cells." Journal of Cell Biology 211, no. 2 (2015): 323–37. http://dx.doi.org/10.1083/jcb.201505123.

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Dynamic microtubules (MTs) continuously explore the intracellular environment and, through specialized plus end–tracking proteins (+TIPs), engage a variety of targets. However, the nature of cargoes that require +TIP-mediated capture for their movement on MTs remains poorly understood. Using RNA interference and dominant-negative approaches, combined with live cell imaging, we show that herpes simplex virus particles that have entered primary human cells exploit a +TIP complex comprising end-binding protein 1 (EB1), cytoplasmic linker protein 170 (CLIP-170), and dynactin-1 (DCTN1) to initiate
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14

Schröder, S., F. Schimmöller, B. Singer-Krüger, and H. Riezman. "The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP." Journal of Cell Biology 131, no. 4 (1995): 895–912. http://dx.doi.org/10.1083/jcb.131.4.895.

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The Saccharomyces cerevisiae EMP47 gene encodes a nonessential type-I transmembrane protein with sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. The 12-amino acid COOH-terminal cytoplasmic tail of Emp47p ends in the sequence KTKLL, which conforms with the consensus for di-lysine-based ER-localization signals. Despite the presence of this motif, Emp47p was shown to be a Golgi protein at steady-state. The di-lysine motif of Emp47p was functional when transplanted onto Ste2p, a plasma membrane protein, conferring ER localization. Nevertheless, the di-lysine mo
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15

Ballensiefen, W., D. Ossipov, and H. D. Schmitt. "Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p." Journal of Cell Science 111, no. 11 (1998): 1507–20. http://dx.doi.org/10.1242/jcs.111.11.1507.

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Vesicle-specific SNAP receptors (v-SNAREs) are believed to cycle between consecutive membrane compartments. The v-SNARE Sec22(Sly2)p mediates the targeting of vesicles between endoplasmic reticulum (ER) and early Golgi of Saccharomyces cerevisiae. To analyze factors involved in targeting of Sec22(Sly2)p, an alpha-factor-tagged Sec22 protein (Sec22-alpha) was employed. Only on reaching the late Golgi, can alpha-factor be cleaved from this hybrid protein by Kex2p, a protease localized in this compartment. In wild-type cells Kex2p-cleavage is observed only when Sec22-alpha is greatly overproduced
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16

Bordallo, Javier, Richard K. Plemper, Andreas Finger, and Dieter H. Wolf. "Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins." Molecular Biology of the Cell 9, no. 1 (1998): 209–22. http://dx.doi.org/10.1091/mbc.9.1.209.

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We have studied components of the endoplasmic reticulum (ER) proofreading and degradation system in the yeast Saccharomyces cerevisiae. Using a der3–1 mutant defective in the degradation of a mutated lumenal protein, carboxypeptidase yscY (CPY*), a gene was cloned which encodes a 64-kDa protein of the ER membrane. Der3p was found to be identical with Hrd1p, a protein identified to be necessary for degradation of HMG-CoA reductase. Der3p contains five putative transmembrane domains and a long hydrophilic C-terminal tail containing a RING-H2 finger domain which is oriented to the ER lumen. Delet
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17

Falk, Julien, Olivier Thoumine, Caroline Dequidt, Daniel Choquet, and Catherine Faivre-Sarrailh. "NrCAM Coupling to the Cytoskeleton Depends on Multiple Protein Domains and Partitioning into Lipid Rafts." Molecular Biology of the Cell 15, no. 10 (2004): 4695–709. http://dx.doi.org/10.1091/mbc.e04-03-0171.

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NrCAM is a cell adhesion molecule of the L1 family that is implicated in the control of axonal growth. Adhesive contacts may promote advance of the growth cone by triggering the coupling of membrane receptors with the F-actin retrograde flow. We sought to understand the mechanisms leading to clutching the F-actin at the site of ligand-mediated clustering of NrCAM. Using optical tweezers and single particle tracking of beads coated with the ligand TAG-1, we analyzed the mobility of NrCAM-deletion mutants transfected in a neuroblastoma cell line. Deletion of the cytoplasmic tail did not prevent
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18

Conibear, Elizabeth, and Tom H. Stevens. "Vps52p, Vps53p, and Vps54p Form a Novel Multisubunit Complex Required for Protein Sorting at the Yeast Late Golgi." Molecular Biology of the Cell 11, no. 1 (2000): 305–23. http://dx.doi.org/10.1091/mbc.11.1.305.

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The late Golgi of the yeast Saccharomyces cerevisiaereceives membrane traffic from the secretory pathway as well as retrograde traffic from post-Golgi compartments, but the machinery that regulates these vesicle-docking and fusion events has not been characterized. We have identified three components of a novel protein complex that is required for protein sorting at the yeast late Golgi compartment. Mutation of VPS52, VPS53, orVPS54 results in the missorting of 70% of the vacuolar hydrolase carboxypeptidase Y as well as the mislocalization of late Golgi membrane proteins to the vacuole, wherea
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Bai, Zhiyong, and Barth D. Grant. "A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling." Proceedings of the National Academy of Sciences 112, no. 12 (2015): E1443—E1452. http://dx.doi.org/10.1073/pnas.1418651112.

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Endosome-to-Golgi transport is required for the function of many key membrane proteins and lipids, including signaling receptors, small-molecule transporters, and adhesion proteins. The retromer complex is well-known for its role in cargo sorting and vesicle budding from early endosomes, in most cases leading to cargo fusion with the trans-Golgi network (TGN). Transport from recycling endosomes to the TGN has also been reported, but much less is understood about the molecules that mediate this transport step. Here we provide evidence that the F-BAR domain proteins TOCA-1 and TOCA-2 (Transducer
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Zhang, Donglei, Nora R. Isack, Doreen R. Glodowski, et al. "RAB-6.2 and the retromer regulate glutamate receptor recycling through a retrograde pathway." Journal of Cell Biology 196, no. 1 (2012): 85–101. http://dx.doi.org/10.1083/jcb.201104141.

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Regulated membrane trafficking of AMPA-type glutamate receptors (AMPARs) is a key mechanism underlying synaptic plasticity, yet the pathways used by AMPARs are not well understood. In this paper, we show that the AMPAR subunit GLR-1 in Caenorhabditis elegans utilizes the retrograde transport pathway to regulate AMPAR synaptic abundance. Mutants for rab-6.2, the retromer genes vps-35 and snx-1, and rme-8 failed to recycle GLR-1 receptors, resulting in GLR-1 turnover and behavioral defects indicative of diminished GLR-1 function. In contrast, expression of constitutively active RAB-6.2 drove the
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Schneider, Karin, and Paul Massa. "SHP-1 regulates neuroinvasion of neurotropic virus into the CNS (VIR5P.1035)." Journal of Immunology 192, no. 1_Supplement (2014): 144.18. http://dx.doi.org/10.4049/jimmunol.192.supp.144.18.

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Abstract Viral infections in the central nervous system (CNS) may have devastating clinical consequences to the host. Neurotropic virus infections often begin in peripheral tissues, which then spread to the CNS via peripheral nerves following entry into nerve terminals by receptor-mediated endocytosis and subsequent retrograde axonal transport into the CNS compartment. In our lab, a possible novel role for the protein tyrosine phosphatase, SHP-1, in regulating neuroinvasion via peripheral nerves of a neurotropic virus (Theiler’s Murine Encephalomyelitis Virus, TMEV) is being investigated. Prel
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Chen, Xu-Qiao, Fang Fang, Jazmin B. Florio, et al. "T-complex protein 1-ring complex enhances retrograde axonal transport by modulating tau phosphorylation." Traffic 19, no. 11 (2018): 840–53. http://dx.doi.org/10.1111/tra.12610.

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Hamada, Yuki, Yuta Tsurumi, Shohei Nozaki, Yohei Katoh, and Kazuhisa Nakayama. "Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the dynein-2 complex is crucial for ciliary protein trafficking." Molecular Biology of the Cell 29, no. 13 (2018): 1628–39. http://dx.doi.org/10.1091/mbc.e18-03-0173.

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The dynein-2 complex mediates trafficking of ciliary proteins by powering the intraflagellar transport (IFT) machinery containing IFT-A and IFT-B complexes. Although 11 subunits are known to constitute the dynein-2 complex, with several light-chain subunits shared by the dynein-1 complex, the overall architecture of the dynein-2 complex has not been fully clarified. Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2–DYNLT1/DYNLT3 dimer. The d
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Buser, Dominik P., Gaétan Bader, and Martin Spiess. "Retrograde transport of CDMPR depends on several machineries as analyzed by sulfatable nanobodies." Life Science Alliance 5, no. 7 (2022): e202101269. http://dx.doi.org/10.26508/lsa.202101269.

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Retrograde protein transport from the cell surface and endosomes to the TGN is essential for membrane homeostasis in general and for the recycling of mannose-6-phosphate receptors (MPRs) for sorting of lysosomal hydrolases in particular. We used a nanobody-based sulfation tool to more directly determine transport kinetics from the plasma membrane to the TGN for the cation-dependent MPR (CDMPR) with and without rapid or gradual inactivation of candidate machinery proteins. Although knockdown of retromer (Vps26), epsinR, or Rab9a reduced CDMPR arrival to the TGN, no effect was observed upon sile
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Li, Guichen, Zitong Li, Zeyun Yang, Yehoram Leshem, Yuequan Shen, and Shuzhen Men. "Mitochondrial heat-shock cognate protein 70 contributes to auxin-mediated embryo development." Plant Physiology 186, no. 2 (2021): 1101–21. http://dx.doi.org/10.1093/plphys/kiab138.

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Abstract In Arabidopsis thaliana, mitochondrial-localized heat-shock cognate protein 70-1 (mtHSC70-1) plays an important role in vegetativegrowth. However, whether mtHSC70-1 affects reproductive growth remains unknown. Here, we found that the mtHSC70-1 gene was expressed in the provascular cells of the embryo proper from the early heart stage onward during embryogenesis. Phenotypic analyses of mthsc70-1 mutants revealed that mtHSC70 deficiency leads to defective embryo development and that this effect is mediated by auxin. In addition to a dwarf phenotype, the mthsc70-1 mutant displayed defect
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Tadini, Luca, Nicolaj Jeran, and Paolo Pesaresi. "GUN1 and Plastid RNA Metabolism: Learning from Genetics." Cells 9, no. 10 (2020): 2307. http://dx.doi.org/10.3390/cells9102307.

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GUN1 (genomes uncoupled 1), a chloroplast-localized pentatricopeptide repeat (PPR) protein with a C-terminal small mutS-related (SMR) domain, plays a central role in the retrograde communication of chloroplasts with the nucleus. This flow of information is required for the coordinated expression of plastid and nuclear genes, and it is essential for the correct development and functioning of chloroplasts. Multiple genetic and biochemical findings indicate that GUN1 is important for protein homeostasis in the chloroplast; however, a clear and unified view of GUN1′s role in the chloroplast is sti
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Chen, Xu-Qiao. "Involvement of T-complex protein 1-ring complex/chaperonin containing T-complex protein 1 (TRiC/CCT) in retrograde axonal transport through tau phosphorylation." Neural Regeneration Research 14, no. 4 (2019): 588. http://dx.doi.org/10.4103/1673-5374.247460.

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Doi, Motomichi, and Kouichi Iwasaki. "Regulation of Retrograde Signaling at Neuromuscular Junctions by the Novel C2 Domain Protein AEX-1." Neuron 33, no. 2 (2002): 249–59. http://dx.doi.org/10.1016/s0896-6273(01)00587-6.

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Brown, Frank C., Carmel H. Schindelhaim, and Suzanne R. Pfeffer. "GCC185 plays independent roles in Golgi structure maintenance and AP-1–mediated vesicle tethering." Journal of Cell Biology 194, no. 5 (2011): 779–87. http://dx.doi.org/10.1083/jcb.201104019.

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GCC185 is a long coiled-coil protein localized to the trans-Golgi network (TGN) that functions in maintaining Golgi structure and tethering mannose 6-phosphate receptor (MPR)–containing transport vesicles en route to the Golgi. We report the identification of two distinct domains of GCC185 needed either for Golgi structure maintenance or transport vesicle tethering, demonstrating the independence of these two functions. The domain needed for vesicle tethering binds to the clathrin adaptor AP-1, and cells depleted of GCC185 accumulate MPRs in transport vesicles that are AP-1 decorated. This stu
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Ye, Guo-Jie, Kevin T. Vaughan, Richard B. Vallee, and Bernard Roizman. "The Herpes Simplex Virus 1 UL34 Protein Interacts with a Cytoplasmic Dynein Intermediate Chain and Targets Nuclear Membrane." Journal of Virology 74, no. 3 (2000): 1355–63. http://dx.doi.org/10.1128/jvi.74.3.1355-1363.2000.

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ABSTRACT To express the function encoded in its genome, the herpes simplex virus 1 capsid-tegument structure released by deenvelopment during entry into cells must be transported retrograde to the nuclear pore where viral DNA is released into the nucleus. This path is essential in the case of virus entering axons of dorsal root ganglia. The objective of the study was to identify the viral proteins that may be involved in the transport. We report the following findings. (i) The neuronal isoform of the intermediate chain (IC-1a) of the dynein complex pulled down, from lysates of [35S]methionine-
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Cavalli, Valeria, Pekka Kujala, Judith Klumperman, and Lawrence S. B. Goldstein. "Sunday Driver links axonal transport to damage signaling." Journal of Cell Biology 168, no. 5 (2005): 775–87. http://dx.doi.org/10.1083/jcb.200410136.

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Neurons transmit long-range biochemical signals between cell bodies and distant axonal sites or termini. To test the hypothesis that signaling molecules are hitchhikers on axonal vesicles, we focused on the c-Jun NH2-terminal kinase (JNK) scaffolding protein Sunday Driver (syd), which has been proposed to link the molecular motor protein kinesin-1 to axonal vesicles. We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex. Nerve injury induces
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Li, Yan, Seung Lim, David Hoffman, Pontus Aspenstrom, Howard J. Federoff та David A. Rempe. "HUMMR, a hypoxia- and HIF-1α–inducible protein, alters mitochondrial distribution and transport". Journal of Cell Biology 185, № 6 (2009): 1065–81. http://dx.doi.org/10.1083/jcb.200811033.

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Mitochondrial transport is critical for maintenance of normal neuronal function. Here, we identify a novel mitochondria protein, hypoxia up-regulated mitochondrial movement regulator (HUMMR), which is expressed in neurons and is markedly induced by hypoxia-inducible factor 1 α (HIF-1α). Interestingly, HUMMR interacts with Miro-1 and Miro-2, mitochondrial proteins that are critical for mediating mitochondrial transport. Interestingly, knockdown of HUMMR or HIF-1 function in neurons exposed to hypoxia markedly reduces mitochondrial content in axons. Because mitochondrial transport and distributi
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Fu, Meng-meng, and Erika L. F. Holzbaur. "JIP1 regulates the directionality of APP axonal transport by coordinating kinesin and dynein motors." Journal of Cell Biology 202, no. 3 (2013): 495–508. http://dx.doi.org/10.1083/jcb.201302078.

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Regulation of the opposing kinesin and dynein motors that drive axonal transport is essential to maintain neuronal homeostasis. Here, we examine coordination of motor activity by the scaffolding protein JNK-interacting protein 1 (JIP1), which we find is required for long-range anterograde and retrograde amyloid precursor protein (APP) motility in axons. We identify novel interactions between JIP1 and kinesin heavy chain (KHC) that relieve KHC autoinhibition, activating motor function in single molecule assays. The direct binding of the dynactin subunit p150Glued to JIP1 competitively inhibits
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Blisnick, Thierry, Johanna Buisson, Sabrina Absalon, Alexandra Marie, Nadège Cayet, and Philippe Bastin. "The intraflagellar transport dynein complex of trypanosomes is made of a heterodimer of dynein heavy chains and of light and intermediate chains of distinct functions." Molecular Biology of the Cell 25, no. 17 (2014): 2620–33. http://dx.doi.org/10.1091/mbc.e14-05-0961.

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Cilia and flagella are assembled by intraflagellar transport (IFT) of protein complexes that bring tubulin and other precursors to the incorporation site at their distal tip. Anterograde transport is driven by kinesin, whereas retrograde transport is ensured by a specific dynein. In the protist Trypanosoma brucei, two distinct genes encode fairly different dynein heavy chains (DHCs; ∼40% identity) termed DHC2.1 and DHC2.2, which form a heterodimer and are both essential for retrograde IFT. The stability of each heavy chain relies on the presence of a dynein light intermediate chain (DLI1; also
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35

Ha, Junghoon, Kevin W. H. Lo, Kenneth R. Myers, et al. "A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes." Journal of Cell Biology 181, no. 6 (2008): 1027–39. http://dx.doi.org/10.1083/jcb.200803150.

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Cytoplasmic dynein is the multisubunit motor protein for retrograde movement of diverse cargoes to microtubule minus ends. Here, we investigate the function of dynein variants, defined by different intermediate chain (IC) isoforms, by expressing fluorescent ICs in neuronal cells. Green fluorescent protein (GFP)–IC incorporates into functional dynein complexes that copurify with membranous organelles. In living PC12 cell neurites, GFP–dynein puncta travel in both the anterograde and retrograde directions. In cultured hippocampal neurons, neurotrophin receptor tyrosine kinase B (TrkB) signaling
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36

Roy, Dheeraj S., Shruti Muralidhar, Lillian M. Smith, and Susumu Tonegawa. "Silent memory engrams as the basis for retrograde amnesia." Proceedings of the National Academy of Sciences 114, no. 46 (2017): E9972—E9979. http://dx.doi.org/10.1073/pnas.1714248114.

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Recent studies identified neuronal ensembles and circuits that hold specific memory information (memory engrams). Memory engrams are retained under protein synthesis inhibition-induced retrograde amnesia. These engram cells can be activated by optogenetic stimulation for full-fledged recall, but not by stimulation using natural recall cues (thus, amnesia). We call this state of engrams “silent engrams” and the cells bearing them “silent engram cells.” The retention of memory information under amnesia suggests that the time-limited protein synthesis following learning is dispensable for memory
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37

Liu, Xian-Dong, Xiao-Na Zhu, Michael M. Halford, Tian-Le Xu, Mark Henkemeyer, and Nan-Jie Xu. "Retrograde regulation of mossy fiber axon targeting and terminal maturation via postsynaptic Lnx1." Journal of Cell Biology 217, no. 11 (2018): 4007–24. http://dx.doi.org/10.1083/jcb.201803105.

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Neuronal connections are initiated by axon targeting to form synapses. However, how the maturation of axon terminals is modulated through interacting with postsynaptic elements remains elusive. In this study, we find that ligand of Numb protein X 1 (Lnx1), a postsynaptic PDZ protein expressed in hippocampal CA3 pyramidal neurons, is essential for mossy fiber (MF) axon targeting during the postnatal period. Lnx1 deletion causes defective synaptic arrangement that leads to aberrant presynaptic terminals. We further identify EphB receptors as novel Lnx1-binding proteins to form a multiprotein com
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38

Pérez-Victoria, F. Javier, Christina Schindler, Javier G. Magadán, et al. "Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex." Molecular Biology of the Cell 21, no. 19 (2010): 3386–95. http://dx.doi.org/10.1091/mbc.e10-05-0392.

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The Golgi-associated retrograde protein (GARP) complex mediates tethering and fusion of endosome-derived transport carriers to the trans-Golgi network (TGN). In the yeast Saccharomyces cerevisiae, GARP comprises four subunits named Vps51p, Vps52p, Vps53p, and Vps54p. Orthologues of the GARP subunits, except for Vps51p, have been identified in all other eukaryotes. A yeast two-hybrid screen of a human cDNA library yielded a phylogenetically conserved protein, Ang2/Fat-free, which interacts with human Vps52, Vps53 and Vps54. Human Ang2 is larger than yeast Vps51p, but exhibits significant homolo
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39

Schroder-Kohne, S., F. Letourneur, and H. Riezman. "Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport." Journal of Cell Science 111, no. 23 (1998): 3459–70. http://dx.doi.org/10.1242/jcs.111.23.3459.

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Emp47p is a yeast Golgi transmembrane protein with a retrograde, Golgi to ER transport di-lysine signal in its cytoplasmic tail. Emp47p has previously been shown to recycle between the Golgi complex and the ER and to require its di-lysine signal for Golgi localization. In contrast to other proteins with di-lysine signals, the Golgi-localization of Emp47p has been shown to be preserved in ret1-1 cells expressing a mutant alpha-COP subunit of coatomer. Here we demonstrate by sucrose gradient fractionation and immunofluorescence analysis that recycling of Emp47p was unimpaired in ret1-1. Furtherm
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40

Saatman, Kathryn E., Babak Abai, Ashley Grosvenor, Christian K. Vorwerk, Douglas H. Smith, and David F. Meaney. "Traumatic Axonal Injury Results in Biphasic Calpain Activation and Retrograde Transport Impairment in Mice." Journal of Cerebral Blood Flow & Metabolism 23, no. 1 (2003): 34–42. http://dx.doi.org/10.1097/01.wcb.0000035040.10031.b0.

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Traumatic axonal injury (TAI) is one of the most important pathologies associated with closed head injury, and contributes to ensuing morbidity. The authors evaluated the potential role of calpains in TAI using a new model of optic nerve stretch injury in mice. Male C57BL/6 mice were anesthetized, surgically prepared, and subjected to a 2.0-mm optic nerve stretch injury (n = 34) or sham injury (n = 18). At various intervals up to 2 weeks after injury, optic nerves were examined for neurofilament proteins and calpain-mediated spectrin breakdown products using immunohistochemistry. In addition,
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41

Rossi, Simona, Michela Di Salvio, Marilisa Balì, et al. "C9orf72 Toxic Species Affect ArfGAP-1 Function." Cells 12, no. 15 (2023): 2007. http://dx.doi.org/10.3390/cells12152007.

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Compelling evidence indicates that defects in nucleocytoplasmic transport contribute to the pathogenesis of amyotrophic lateral sclerosis (ALS). In particular, hexanucleotide (G4C2) repeat expansions in C9orf72, the most common cause of genetic ALS, have a widespread impact on the transport machinery that regulates the nucleocytoplasmic distribution of proteins and RNAs. We previously reported that the expression of G4C2 hexanucleotide repeats in cultured human and mouse cells caused a marked accumulation of poly(A) mRNAs in the cell nuclei. To further characterize the process, we set out to s
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42

Zhang, Xingmin, Shan Jiang, Kelly A. Mitok, Lingjun Li, Alan D. Attie, and Thomas F. J. Martin. "BAIAP3, a C2 domain–containing Munc13 protein, controls the fate of dense-core vesicles in neuroendocrine cells." Journal of Cell Biology 216, no. 7 (2017): 2151–66. http://dx.doi.org/10.1083/jcb.201702099.

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Dense-core vesicle (DCV) exocytosis is a SNARE (soluble N-ethylmaleimide–sensitive fusion attachment protein receptor)-dependent anterograde trafficking pathway that requires multiple proteins for regulation. Several C2 domain–containing proteins are known to regulate Ca2+-dependent DCV exocytosis in neuroendocrine cells. In this study, we identified others by screening all (∼139) human C2 domain–containing proteins by RNA interference in neuroendocrine cells. 40 genes were identified, including several encoding proteins with known roles (CAPS [calcium-dependent activator protein for secretion
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43

Uchida, Atsuko, and Anthony Brown. "Arrival, Reversal, and Departure of Neurofilaments at the Tips of Growing Axons." Molecular Biology of the Cell 15, no. 9 (2004): 4215–25. http://dx.doi.org/10.1091/mbc.e04-05-0371.

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We have investigated the movement of green fluorescent protein-tagged neurofilaments at the distal ends of growing axons by using time-lapse fluorescence imaging. The filaments moved in a rapid, infrequent, and asynchronous manner in either an anterograde or retrograde direction (60% anterograde, 40% retrograde). Most of the anterograde filaments entered the growth cone and most of the retrograde filaments originated in the growth cone. In a small number of cases we were able to observe neurofilaments reverse direction, and all of these reversals occurred in or close to the growth cone. We con
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44

Jacobsen, Björn, Christian Freichel, Anne Eichinger-Chapelon та ін. "Drug-induced Obstructive and Retrograde Nephropathy Associated with α2u-globulin in Male Rats". Toxicologic Pathology 47, № 2 (2018): 138–49. http://dx.doi.org/10.1177/0192623318816039.

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The chemically induced accumulation of α2u-globulin protein in male rats causes specific renal lesions and subsequent nephropathy. Herein, we report additional parallel findings in the kidney of male rats consistent with obstructive and retrograde nephropathy. Kidney and urinary bladder samples were evaluated from Wistar rats treated with RG7129 for 2 week and 8 week and from an 8-week mechanistic study using females, intact and castrated males. Histopathological findings were present in intact males in all studies, including hyaline droplet accumulation and granular casts consistent with α2u-
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45

Natsume, Waka, Kenji Tanabe, Shunsuke Kon, et al. "SMAP2, a Novel ARF GTPase-activating Protein, Interacts with Clathrin and Clathrin Assembly Protein and Functions on the AP-1–positive Early Endosome/Trans-Golgi Network." Molecular Biology of the Cell 17, no. 6 (2006): 2592–603. http://dx.doi.org/10.1091/mbc.e05-10-0909.

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We recently reported that SMAP1, a GTPase-activating protein (GAP) for Arf6, directly interacts with clathrin and regulates the clathrin-dependent endocytosis of transferrin receptors from the plasma membrane. Here, we identified a SMAP1 homologue that we named SMAP2. Like SMAP1, SMAP2 exhibits GAP activity and interacts with clathrin heavy chain (CHC). Furthermore, we show that SMAP2 interacts with the clathrin assembly protein CALM. Unlike SMAP1, however, SMAP2 appears to be a regulator of Arf1 in vivo, because cells transfected with a GAP-negative SMAP2 mutant were resistant to brefeldin A.
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46

Lakatos, Lőrincz, Szabó, et al. "Sec20 is Required for Autophagic and Endocytic Degradation Independent of Golgi-ER Retrograde Transport." Cells 8, no. 8 (2019): 768. http://dx.doi.org/10.3390/cells8080768.

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Endocytosis and autophagy are evolutionarily conserved degradative processes in all eukaryotes. Both pathways converge to the lysosome where cargo is degraded. Improper lysosomal degradation is observed in many human pathologies, so its regulatory mechanisms are important to understand. Sec20/BNIP1 (BCL2/adenovirus E1B 19 kDa protein-interacting protein 1) is a BH3 (Bcl-2 homology 3) domain-containing SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptors) protein that has been suggested to promote Golgi-ER retrograde transport, mitochondrial fission, apoptosis and mitop
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47

Pathak, Gunja K., Hannah Ornstein, Helim Aranda-Espinoza, Amy J. Karlsson, and Sameer B. Shah. "Increases in Retrograde Injury Signaling Complex-Related Transcripts in Central Axons following Injury." Neural Plasticity 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/3572506.

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Axons in the peripheral nervous system respond to injury by activating retrograde injury signaling (RIS) pathways, which promote local axonal protein synthesis (LPS) and neuronal regeneration. RIS is also initiated following injury of neurons in the central nervous system (CNS). However, regulation of the localization of axonal mRNA required for LPS is not well understood. We used a hippocampal explant system to probe the regulation of axonal levels of RIS-associated transcripts following axonal injury. Axonal levels of importinβ1 and RanBP1 were elevated biphasically at 1 and 24 hrs after axo
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48

Aoki, Takehiro, Sarah Ichimura, Ayano Itoh, et al. "Identification of the Neuroblastoma-amplified Gene Product as a Component of the Syntaxin 18 Complex Implicated in Golgi-to-Endoplasmic Reticulum Retrograde Transport." Molecular Biology of the Cell 20, no. 11 (2009): 2639–49. http://dx.doi.org/10.1091/mbc.e08-11-1104.

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Syntaxin 18, a soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) protein implicated in endoplasmic reticulum (ER) membrane fusion, forms a complex with other SNAREs (BNIP1, p31, and Sec22b) and several peripheral membrane components (Sly1, ZW10, and RINT-1). In the present study, we showed that a peripheral membrane protein encoded by the neuroblastoma-amplified gene (NAG) is a subunit of the syntaxin 18 complex. NAG encodes a protein of 2371 amino acids, which exhibits weak similarity to yeast Dsl3p/Sec39p, an 82-kDa component of the complex containing the ye
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49

Aras, Siddhesh, Neeraja Purandare, Stephanie Gladyck, et al. "Mitochondrial Nuclear Retrograde Regulator 1 (MNRR1) rescues the cellular phenotype of MELAS by inducing homeostatic mechanisms." Proceedings of the National Academy of Sciences 117, no. 50 (2020): 32056–65. http://dx.doi.org/10.1073/pnas.2005877117.

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MNRR1 (CHCHD2) is a bi-organellar regulator of mitochondrial function that directly activates cytochrome c oxidase in the mitochondria and functions in the nucleus as a transcriptional activator for hundreds of genes. Since MNRR1 depletion contains features of a mitochondrial disease phenotype, we evaluated the effects of forced expression of MNRR1 on the mitochondrial disease MELAS (mitochondrial encephalomyopathy, lactic acidosis and stroke-like episodes) syndrome. MELAS is a multisystem encephalomyopathy disorder that can result from a heteroplasmic mutation in the mitochondrial DNA (mtDNA;
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50

Davis, R. H., and J. R. Mathias. "Phorbol esters induce retrograde myoelectric activity in rabbit ileum in vivo." American Journal of Physiology-Gastrointestinal and Liver Physiology 257, no. 4 (1989): G578—G583. http://dx.doi.org/10.1152/ajpgi.1989.257.4.g578.

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We demonstrated a unique myoelectric response to phorbol esters and a diacylglycerol, 1-oleoyl-2-acetyl-snglycerol, in rabbit ileal loops. This retrograde activity, the orad migrating complex (OMC), was devoid of slow-wave distortion or alterations in slow-wave frequency. The OMC was not inhibited by the cyclooxygenase inhibitor indomethacin or enhanced by addition of the calcium ionophore A23187. The OMC occurred after 4 beta-phorbol 12-myristate 13-acetate, a phorbol ester known to activate protein kinase C, and after 4 alpha-phorbol 12,13-didecanoate, one that does not. Therefore, these stu
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