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Journal articles on the topic 'Dynein'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Jha, Rupam, and Thomas Surrey. "Regulation of processive motion and microtubule localization of cytoplasmic dynein." Biochemical Society Transactions 43, no. 1 (2015): 48–57. http://dx.doi.org/10.1042/bst20140252.

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The cytoplasmic dynein complex is the major minus-end-directed microtubule motor. Although its directionality is evolutionary well conserved, differences exist among cytoplasmic dyneins from different species in their stepping behaviour, maximum velocity and force production. Recent experiments also suggest differences in processivity regulation. In the present article, we give an overview of dynein's motile properties, with a special emphasis on processivity and its regulation. Furthermore, we summarize recent findings of different pathways for microtubule plus-end loading of dynein. The pres

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2

Ishibashi, Kenta, Hitoshi Sakakibara, and Kazuhiro Oiwa. "Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble." International Journal of Molecular Sciences 21, no. 8 (2020): 2843. http://dx.doi.org/10.3390/ijms21082843.

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In eukaryotic cilia and flagella, various types of axonemal dyneins orchestrate their distinct functions to generate oscillatory bending of axonemes. The force-generating mechanism of dyneins has recently been well elucidated, mainly in cytoplasmic dyneins, thanks to progress in single-molecule measurements, X-ray crystallography, and advanced electron microscopy. These techniques have shed light on several important questions concerning what conformational changes accompany ATP hydrolysis and whether multiple motor domains are coordinated in the movements of dynein. However, due to the lack o

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3

Rao, Lu, and Arne Gennerich. "Structure and Function of Dynein’s Non-Catalytic Subunits." Cells 13, no. 4 (2024): 330. http://dx.doi.org/10.3390/cells13040330.

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Dynein, an ancient microtubule-based motor protein, performs diverse cellular functions in nearly all eukaryotic cells, with the exception of land plants. It has evolved into three subfamilies—cytoplasmic dynein-1, cytoplasmic dynein-2, and axonemal dyneins—each differentiated by their cellular functions. These megadalton complexes consist of multiple subunits, with the heavy chain being the largest subunit that generates motion and force along microtubules by converting the chemical energy of ATP hydrolysis into mechanical work. Beyond this catalytic core, the functionality of dynein is signi

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4

Yoshida, T., H. Takanari, and K. Izutsu. "Distribution of cytoplasmic and axonemal dyneins in rat tissues." Journal of Cell Science 101, no. 3 (1992): 579–87. http://dx.doi.org/10.1242/jcs.101.3.579.

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Microtubule-associated protein 1C (MAP 1C) is now defined as brain cytoplasmic dynein. Recent studies have suggested that cytoplasmic dynein is a motor protein responsible for the intracellular microtubule-based motility in neuronal and non-neuronal cells. We have prepared an antibody against bovine brain MAP 1C and have examined the localizations of cytoplasmic dynein in rat tissues. Immunoblots of extracts from the tissues showed that the dynein was present in brain, testis, liver, kidney and lung. Immunohistochemical experiments have demonstrated that dynein is localized in Purkinje cells o

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5

Vale, R. D., and Y. Y. Toyoshima. "Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia." Journal of Cell Biology 108, no. 6 (1989): 2327–34. http://dx.doi.org/10.1083/jcb.108.6.2327.

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Tetrahymena cilia contain a three-headed 22S (outer arm) dynein and a single-headed 14S dynein. In this study, we have employed an in vitro assay of microtubule translocation along dynein-coated glass surfaces to characterize the motile properties of 14S dynein, 22S dynein, and proteolytic fragments of 22S dynein. Microtubule translocation produced by intact 22S dynein and 14S dynein differ in a number of respects including (a) the maximal velocities of movement; (b) the ability of 22S dynein but not 14S dynein to utilize ATP gamma S to induce movement; (c) the optimal pH and ionic conditions

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6

Sanghavi, Paulomi, Pankaj Kumar, Ankit Roy, M. S. Madhusudhan, and Roop Mallik. "On and off controls within dynein–dynactin on native cargoes." Proceedings of the National Academy of Sciences 118, no. 23 (2021): e2103383118. http://dx.doi.org/10.1073/pnas.2103383118.

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The dynein–dynactin nanomachine transports cargoes along microtubules in cells. Why dynactin interacts separately with the dynein motor and also with microtubules is hotly debated. Here we disrupted these interactions in a targeted manner on phagosomes extracted from cells, followed by optical trapping to interrogate native dynein–dynactin teams on single phagosomes. Perturbing the dynactin–dynein interaction reduced dynein’s on rate to microtubules. In contrast, perturbing the dynactin–microtubule interaction increased dynein’s off rate markedly when dynein was generating force against the op

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7

Yamamoto, Ryosuke, Kangkang Song, Haru-aki Yanagisawa, et al. "The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility." Journal of Cell Biology 201, no. 2 (2013): 263–78. http://dx.doi.org/10.1083/jcb.201211048.

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Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain compl

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8

Asai, D. J., S. M. Beckwith, K. A. Kandl, H. H. Keating, H. Tjandra, and J. D. Forney. "The dynein genes of Paramecium tetraurelia. Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms." Journal of Cell Science 107, no. 4 (1994): 839–47. http://dx.doi.org/10.1242/jcs.107.4.839.

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Paramecium tetraurelia is a unicellular organism that utilizes both axonemal and cytoplasmic dyneins. The highly conserved region containing the catalytic P-loop of the dynein heavy chain was amplified by RNA-directed polymerase chain reaction. Eight different P-loop-containing cDNA fragments were cloned. Southern hybridization analysis indicated that each fragment corresponds to a separate dynein gene and that there are at least 12 dynein heavy chain genes expressed in Paramecium. Seven of the eight cloned contain sequence motif A, which is found in axonemal dyneins, and one contains sequence

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9

Canty, John T., Ruensern Tan, Emre Kusakci, Jonathan Fernandes, and Ahmet Yildiz. "Structure and Mechanics of Dynein Motors." Annual Review of Biophysics 50, no. 1 (2021): 549–74. http://dx.doi.org/10.1146/annurev-biophys-111020-101511.

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Dyneins make up a family of AAA+ motors that move toward the minus end of microtubules. Cytoplasmic dynein is responsible for transporting intracellular cargos in interphase cells and mediating spindle assembly and chromosome positioning during cell division. Other dynein isoforms transport cargos in cilia and power ciliary beating. Dyneins were the least studied of the cytoskeletal motors due to challenges in the reconstitution of active dynein complexes in vitro and the scarcity of high-resolution methods for in-depth structural and biophysical characterization of these motors. These challen

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10

Roberts, Anthony J. "Emerging mechanisms of dynein transport in the cytoplasm versus the cilium." Biochemical Society Transactions 46, no. 4 (2018): 967–82. http://dx.doi.org/10.1042/bst20170568.

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Two classes of dynein power long-distance cargo transport in different cellular contexts. Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior. Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella. Both dyneins operate as large ATP-driven motor complexes, whose dysfunction is associated with a group of human disorders. But how similar are their mechanisms of action and regulation? To examine this question, this review focuses on recent advances in dynein-1 and -2

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11

Antony, Dinu, Han G. Brunner, and Miriam Schmidts. "Ciliary Dyneins and Dynein Related Ciliopathies." Cells 10, no. 8 (2021): 1885. http://dx.doi.org/10.3390/cells10081885.

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Although ubiquitously present, the relevance of cilia for vertebrate development and health has long been underrated. However, the aberration or dysfunction of ciliary structures or components results in a large heterogeneous group of disorders in mammals, termed ciliopathies. The majority of human ciliopathy cases are caused by malfunction of the ciliary dynein motor activity, powering retrograde intraflagellar transport (enabled by the cytoplasmic dynein-2 complex) or axonemal movement (axonemal dynein complexes). Despite a partially shared evolutionary developmental path and shared ciliary

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12

Kandl, K. A., J. D. Forney, and D. J. Asai. "The dynein genes of Paramecium tetraurelia: the structure and expression of the ciliary beta and cytoplasmic heavy chains." Molecular Biology of the Cell 6, no. 11 (1995): 1549–62. http://dx.doi.org/10.1091/mbc.6.11.1549.

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The genes encoding two Paramecium dynein heavy chains, DHC-6 and DHC-8, have been cloned and sequenced. Sequence-specific antibodies demonstrate that DHC-6 encodes ciliary outer arm beta-chain and DHC-8 encodes a cytoplasmic dynein heavy chain. Therefore, this study is the first opportunity to compare the primary structures and expression of two heavy chains representing the two functional classes of dynein expressed in the same cell. Deciliation of paramecia results in the accumulation of mRNA from DHC-6, but not DHC-8. Nuclear run-on transcription experiments demonstrate that this increase i

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13

Wirschell, Maureen, Chun Yang, Pinfen Yang, et al. "IC97 Is a Novel Intermediate Chain of I1 Dynein That Interacts with Tubulin and Regulates Interdoublet Sliding." Molecular Biology of the Cell 20, no. 13 (2009): 3044–54. http://dx.doi.org/10.1091/mbc.e09-04-0276.

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Our goal is to understand the assembly and regulation of flagellar dyneins, particularly the Chlamydomonas inner arm dynein called I1 dynein. Here, we focus on the uncharacterized I1-dynein IC IC97. The IC97 gene encodes a novel IC without notable structural domains. IC97 shares homology with the murine lung adenoma susceptibility 1 (Las1) protein—a candidate tumor suppressor gene implicated in lung tumorigenesis. Multiple, independent biochemical assays determined that IC97 interacts with both α- and β-tubulin subunits within the axoneme. I1-dynein assembly mutants suggest that IC97 interacts

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14

Wang, Limei, Xuecheng Li, Guang Liu, and Junmin Pan. "FBB18 participates in preassembly of almost all axonemal dyneins ind of R2TP complex." PLOS Genetics 18, no. 8 (2022): e1010374. http://dx.doi.org/10.1371/journal.pgen.1010374.

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Assembly of dynein arms requires cytoplasmic processes which are mediated by dynein preassembly factors (DNAAFs). CFAP298, which is conserved in organisms with motile cilia, is required for assembly of dynein arms but with obscure mechanisms. Here, we show that FBB18, a Chlamydomonas homologue of CFAP298, localizes to the cytoplasm and functions in folding/stabilization of almost all axonemal dyneins at the early steps of dynein preassembly. Mutation of FBB18 causes no or short cilia accompanied with partial loss of both outer and inner dynein arms. Comparative proteomics using 15N labeling su

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15

Criswell, P. S., L. E. Ostrowski, and D. J. Asai. "A novel cytoplasmic dynein heavy chain: expression of DHC1b in mammalian ciliated epithelial cells." Journal of Cell Science 109, no. 7 (1996): 1891–98. http://dx.doi.org/10.1242/jcs.109.7.1891.

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Organisms that have cilia or flagella express over a dozen dynein heavy chain genes. Of these heavy chain genes, most appear to encode axonemal dyneins, one encodes conventional cytoplasmic dynein (MAP1C or DHC1a), and one, here referred to as DHC1b, encodes an unclassified heavy chain. Previous analysis of sea urchin DHC1b (Gibbons et al. (1994) Mol. Biol. Cell 5, 57–70) indicated that this isoform is either an axonemal dynein with an unusual protein sequence or a cytoplasmic dynein whose expression increases during ciliogenesis. In the present study, we examined the expression of DHC1b in ra

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16

Wilkerson, C. G., S. M. King, and G. B. Witman. "Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein." Journal of Cell Science 107, no. 3 (1994): 497–506. http://dx.doi.org/10.1242/jcs.107.3.497.

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We report here the complete sequence of the gamma dynein heavy chain of the outer arm of the Chlamydomonas flagellum, and partial sequences for six other dynein heavy chains. The gamma dynein heavy chain sequence contains four P-loop motifs, one of which is the likely hydrolytic site based on its position relative to a previously mapped epitope. Comparison with available cytoplasmic and flagellar dynein heavy chain sequences reveals regions that are highly conserved in all dynein heavy chains sequenced to date, regions that are conserved only among axonemal dynein heavy chains, and regions tha

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17

King, Stephen M., and Winfield S. Sale. "Fifty years of microtubule sliding in cilia." Molecular Biology of the Cell 29, no. 6 (2018): 698–701. http://dx.doi.org/10.1091/mbc.e17-07-0483.

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Motility of cilia (also known as flagella in some eukaryotes) is based on axonemal doublet microtubule sliding that is driven by the dynein molecular motors. Dyneins are organized into intricately patterned inner and outer rows of arms, whose collective activity is to produce inter-microtubule movement. However, to generate a ciliary bend, not all dyneins can be active simultaneously. The switch point model accounts, in part, for how dynein motors are regulated during ciliary movement. On the basis of this model, supported by key direct experimental observations as well as more recent theoreti

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18

Lee, Seungwon, Julie C. Wisniewski, William L. Dentler, and David J. Asai. "Gene Knockouts Reveal Separate Functions for Two Cytoplasmic Dyneins in Tetrahymena thermophila." Molecular Biology of the Cell 10, no. 3 (1999): 771–84. http://dx.doi.org/10.1091/mbc.10.3.771.

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In many organisms, there are multiple isoforms of cytoplasmic dynein heavy chains, and division of labor among the isoforms would provide a mechanism to regulate dynein function. The targeted disruption of somatic genes in Tetrahymena thermophilapresents the opportunity to determine the contributions of individual dynein isoforms in a single cell that expresses multiple dynein heavy chain genes. Substantial portions of twoTetrahymena cytoplasmic dynein heavy chain genes were cloned, and their motor domains were sequenced. Tetrahymena DYH1 encodes the ubiquitous cytoplasmic dynein Dyh1, andDYH2

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19

Yamamoto, Ryosuke, Haru-aki Yanagisawa, Toshiki Yagi, and Ritsu Kamiya. "Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from Chlamydomonas to Mammals." Eukaryotic Cell 7, no. 1 (2007): 154–61. http://dx.doi.org/10.1128/ec.00341-07.

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ABSTRACT Cilia and flagella have multiple dyneins in their inner and outer arms. Chlamydomonas inner-arm dynein contains at least seven major subspecies (dynein a to dynein g), of which all but dynein f (also called dynein I1) are the single-headed type that are composed of a single heavy chain, actin, and either centrin or a 28-kDa protein (p28). Dynein d was found to associate with two additional proteins of 38 kDa (p38) and 44 kDa (p44). Following the characterization of the p38 protein (R. Yamamoto, H. A. Yanagisawa, T. Yagi, and R. Kamiya, FEBS Lett. 580:6357-6360, 2006), we have identifi

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20

Mitchell, D. R., and K. S. Brown. "Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain genes." Journal of Cell Science 107, no. 3 (1994): 635–44. http://dx.doi.org/10.1242/jcs.107.3.635.

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We have sequenced genomic clones spanning the complete coding region of one heavy chain (beta) and the catalytic domain of a second (alpha) of the Chlamydomonas reinhardtii flagellar outer arm dynein ATPase. The beta heavy chain gene (ODA-4 locus) spans 20 kb, is divided into at least 30 exons, and encodes a predicted 520 kDa protein. Comparison with sea urchin beta dynein sequences reveals homology that extends throughout both proteins. Over the most conserved central catalytic region, the Chlamydomonas alpha and beta chains are equally divergent from the sea urchin beta chain (64% and 65% si

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21

DiBella, Linda M., Miho Sakato, Ramila S. Patel-King, Gregory J. Pazour, and Stephen M. King. "The LC7 Light Chains of Chlamydomonas Flagellar Dyneins Interact with Components Required for Both Motor Assembly and Regulation." Molecular Biology of the Cell 15, no. 10 (2004): 4633–46. http://dx.doi.org/10.1091/mbc.e04-06-0461.

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Members of the LC7/Roadblock family of light chains (LCs) have been found in both cytoplasmic and axonemal dyneins. LC7a was originally identified within Chlamydomonas outer arm dynein and associates with this motor's cargo-binding region. We describe here a novel member of this protein family, termed LC7b that is also present in the Chlamydomonas flagellum. Levels of LC7b are reduced ∼20% in axonemes isolated from strains lacking inner arm I1 and are ∼80% lower in the absence of the outer arms. When both dyneins are missing, LC7b levels are diminished to <10%. In oda9 axonemal extracts tha

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22

Pfister, K. Kevin, Elizabeth M. C. Fisher, Ian R. Gibbons, et al. "Cytoplasmic dynein nomenclature." Journal of Cell Biology 171, no. 3 (2005): 411–13. http://dx.doi.org/10.1083/jcb.200508078.

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A variety of names has been used in the literature for the subunits of cytoplasmic dynein complexes. Thus, there is a strong need for a more definitive consensus statement on nomenclature. This is especially important for mammalian cytoplasmic dyneins, many subunits of which are encoded by multiple genes. We propose names for the mammalian cytoplasmic dynein subunit genes and proteins that reflect the phylogenetic relationships of the genes and the published studies clarifying the functions of the polypeptides. This nomenclature recognizes the two distinct cytoplasmic dynein complexes and has

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23

Hays, T. S., M. E. Porter, M. McGrail, et al. "A cytoplasmic dynein motor in Drosophila: identification and localization during embryogenesis." Journal of Cell Science 107, no. 6 (1994): 1557–69. http://dx.doi.org/10.1242/jcs.107.6.1557.

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We have characterized a cytoplasmic dynein motor isoform that is present in extracts of Drosophila embryos. A prominent high molecular weight (HMW) polypeptide (&gt; 400 kDa) is enriched in microtubules prepared from nucleotide-depleted embryonic extracts. Based on its ATP-sensitive microtubule binding activity, 20 S sedimentation coefficient, sensitivity to UV-vanadate and nucleotide specificity, the HMW polypeptide resembles cytoplasmic dyneins prepared from other organisms. The Drosophila cytoplasmic dynein acts as a minus-end motor that promotes microtubule translocation in vitro. A po

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Rasmusson, K., M. Serr, J. Gepner, I. Gibbons, and T. S. Hays. "A family of dynein genes in Drosophila melanogaster." Molecular Biology of the Cell 5, no. 1 (1994): 45–55. http://dx.doi.org/10.1091/mbc.5.1.45.

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We report the identification and initial characterization of seven Drosophila dynein heavy chain genes. Each gene is single copy and maps to a unique genomic location. Sequence analysis of partial clones reveals that each encodes a highly conserved portion of the putative dynein hydrolytic ATP-binding site in dyneins that includes a consensus phosphate-binding (P-loop) motif. One of the clones is derived from a Drosophila cytoplasmic dynein heavy chain gene, Dhc64C, that shows extensive amino acid identity to cytoplasmic dynein isoforms from other organisms. Two other Drosophila dynein clones

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Rodriguez-Garcia, Ruddi, Laurent Chesneau, Sylvain Pastezeur, Julien Roul, Marc Tramier, and Jacques Pécréaux. "The polarity-induced force imbalance inCaenorhabditis elegansembryos is caused by asymmetric binding rates of dynein to the cortex." Molecular Biology of the Cell 29, no. 26 (2018): 3093–104. http://dx.doi.org/10.1091/mbc.e17-11-0653.

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During asymmetric cell division, the molecular motor dynein generates cortical pulling forces that position the spindle to reflect polarity and adequately distribute cell fate determinants. In Caenorhabditis elegans embryos, despite a measured anteroposterior force imbalance, antibody staining failed to reveal dynein enrichment at the posterior cortex, suggesting a transient localization there. Dynein accumulates at the microtubule plus ends, in an EBP-2EB–dependent manner. This accumulation, although not transporting dynein, contributes modestly to cortical forces. Most dyneins may instead di

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Gibbons, B. H., D. J. Asai, W. J. Tang, T. S. Hays, and I. R. Gibbons. "Phylogeny and expression of axonemal and cytoplasmic dynein genes in sea urchins." Molecular Biology of the Cell 5, no. 1 (1994): 57–70. http://dx.doi.org/10.1091/mbc.5.1.57.

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Transcripts approximately 14.5 kilobases in length from 14 different genes that encode for dynein heavy chains have been identified in poly(A)+ RNA from sea urchin embryos. Analysis of the changes in level of these dynein transcripts in response to deciliation, together with their sequence relatedness, suggests that 11 or more of these genes encode dynein isoforms that participate in regeneration of external cilia on the embryo, whereas the single gene whose deduced sequence closely resembles that of cytoplasmic dynein in other organisms appears not to be involved in this regeneration. The fou

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Tan, Kaeling, Anthony J. Roberts, Mark Chonofsky, Martin J. Egan, and Samara L. Reck-Peterson. "A microscopy-based screen employing multiplex genome sequencing identifies cargo-specific requirements for dynein velocity." Molecular Biology of the Cell 25, no. 5 (2014): 669–78. http://dx.doi.org/10.1091/mbc.e13-09-0557.

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The timely delivery of membranous organelles and macromolecules to specific locations within the majority of eukaryotic cells depends on microtubule-based transport. Here we describe a screening method to identify mutations that have a critical effect on intracellular transport and its regulation using mutagenesis, multicolor-fluorescence microscopy, and multiplex genome sequencing. This screen exploits the filamentous fungus Aspergillus nidulans, which has many of the advantages of yeast molecular genetics but uses long-range microtubule-based transport in a manner more similar to metazoan ce

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Bui, Khanh Huy, Hitoshi Sakakibara, Tandis Movassagh, Kazuhiro Oiwa, and Takashi Ishikawa. "Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella." Journal of Cell Biology 186, no. 3 (2009): 437–46. http://dx.doi.org/10.1083/jcb.200903082.

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Although the widely shared “9 + 2” structure of axonemes is thought to be highly symmetrical, axonemes show asymmetrical bending during planar and conical motion. In this study, using electron cryotomography and single particle averaging, we demonstrate an asymmetrical molecular arrangement of proteins binding to the nine microtubule doublets in Chlamydomonas reinhardtii flagella. The eight inner arm dynein heavy chains regulate and determine flagellar waveform. Among these, one heavy chain (dynein c) is missing on one microtubule doublet (this doublet also lacks the outer dynein arm), and ano

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Ahmed, Noveera T., and David R. Mitchell. "ODA16p, a Chlamydomonas Flagellar Protein Needed for Dynein Assembly." Molecular Biology of the Cell 16, no. 10 (2005): 5004–12. http://dx.doi.org/10.1091/mbc.e05-07-0627.

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Dynein motors of cilia and flagella function in the context of the axoneme, a very large network of microtubules and associated proteins. To understand how dyneins assemble and attach to this network, we characterized two Chlamydomonas outer arm dynein assembly (oda) mutants at a new locus, ODA16. Both oda16 mutants display a reduced beat frequency and altered swimming behavior, similar to previously characterized oda mutants, but only a partial loss of axonemal dyneins as shown by both electron microscopy and immunoblots. Motility studies suggest that the remaining outer arm dyneins on oda16

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Warner, F. D., J. G. Perreault, and J. H. McIlvain. "Rebinding of Tetrahymena 13 S and 21 S dynein ATPases to extracted doublet microtubules. The inner row and outer row dynein arms." Journal of Cell Science 77, no. 1 (1985): 263–87. http://dx.doi.org/10.1242/jcs.77.1.263.

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Ciliary axonemes from Tetrahymena contain a second salt-extractable ATPase distinguishable from outer arm 21 S dynein by sedimentation velocity (congruent to 13 S), electrophoretic mobility and substrate specificity. As characterized by turbidimetric assay, gel electrophoresis in the presence of sodium dodecyl sulphate, ATPase activity and electron microscopy, the 13 S dynein ATPase rebinds to extracted doublet microtubules. Compared to structural-side (ATP-insensitive) 21 S dynein binding, which is moderately specific for the 24 nm outer row arm position, rebinding of 13 S dynein is highly sp

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Bui, Khanh Huy, Hitoshi Sakakibara, Tandis Movassagh, Kazuhiro Oiwa, and Takashi Ishikawa. "Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella." Journal of Cell Biology 183, no. 5 (2008): 923–32. http://dx.doi.org/10.1083/jcb.200808050.

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The inner dynein arm regulates axonemal bending motion in eukaryotes. We used cryo-electron tomography to reconstruct the three-dimensional structure of inner dynein arms from Chlamydomonas reinhardtii. All the eight different heavy chains were identified in one 96-nm periodic repeat, as expected from previous biochemical studies. Based on mutants, we identified the positions of the AAA rings and the N-terminal tails of all the eight heavy chains. The dynein f dimer is located close to the surface of the A-microtubule, whereas the other six heavy chain rings are roughly colinear at a larger di

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Habermann, A., T. A. Schroer, G. Griffiths, and J. K. Burkhardt. "Immunolocalization of cytoplasmic dynein and dynactin subunits in cultured macrophages: enrichment on early endocytic organelles." Journal of Cell Science 114, no. 1 (2001): 229–40. http://dx.doi.org/10.1242/jcs.114.1.229.

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Cytoplasmic dyneins and their cofactor, dynactin, work together to mediate the movement of numerous cargo organelles toward the minus-ends of microtubules. In many cases, there is compelling evidence that dynactin functions in part to attach dyneins to cargo organelles, but this may not always be the case. We have localized three dynactin subunits (Arp1, p62 and p150(Glued)) and two subunits of conventional cytoplasmic dynein (dynein intermediate chain and dynein heavy chain 1) in murine macrophages using immunogold labeling of thawed cryosections. Using stereological techniques, we have quant

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Smith, E. F., and W. S. Sale. "Structural and functional reconstitution of inner dynein arms in Chlamydomonas flagellar axonemes." Journal of Cell Biology 117, no. 3 (1992): 573–81. http://dx.doi.org/10.1083/jcb.117.3.573.

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The inner row of dynein arms contains three dynein subforms. Each is distinct in composition and location in flagellar axonemes. To begin investigating the specificity of inner dynein arm assembly, we assessed the capability of isolated inner arm dynein subforms to rebind to their appropriate positions on axonemal doublet microtubules by recombining them with either mutant or extracted axonemes missing some or all dyneins. Densitometry of Coomassie blue-stained polyacrylamide gels revealed that for each inner dynein arm subform, binding to axonemes was saturable and stoichiometric. Using struc

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Andrews, K. L., P. Nettesheim, D. J. Asai, and L. E. Ostrowski. "Identification of seven rat axonemal dynein heavy chain genes: expression during ciliated cell differentiation." Molecular Biology of the Cell 7, no. 1 (1996): 71–79. http://dx.doi.org/10.1091/mbc.7.1.71.

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Axonemal dyneins are molecular motors that drive the beating of cilia and flagella. We report here the identification and partial cloning of seven unique axonemal dynein heavy chains from rat tracheal epithelial (RTE) cells. Combinations of axonemal-specific and degenerate primers to conserved regions around the catalytic site of dynein heavy chains were used to obtain cDNA fragments of rat dynein heavy chains. Southern analysis indicates that these are single copy genes, with one possible exception, and Northern analysis of RNA from RTE cells shows a transcript of approximately 15 kb for each

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Vaisberg, E. A., P. M. Grissom, and J. R. McIntosh. "Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles." Journal of Cell Biology 133, no. 4 (1996): 831–42. http://dx.doi.org/10.1083/jcb.133.4.831.

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We describe two dynein heavy chain (DHC)-like polypeptides (DHCs 2 and 3) that are distinct from the heavy chain of conventional cytoplasmic dynein (DHC1) but are expressed in a variety of mammalian cells that lack axonemes. DHC2 is a distant member of the "cytoplasmic" branch of the dynein phylogenetic tree, while DHC3 shares more sequence similarity with dynein-like polypeptides that have been thought to be axonemal. Each cytoplasmic dynein is associated with distinct cellular organelles. DHC2 is localized predominantly to the Golgi apparatus. Moreover, the Golgi disperses upon microinjectio

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Criswell, Peggy S., and David J. Asai. "Evidence for Four Cytoplasmic Dynein Heavy Chain Isoforms in Rat Testis." Molecular Biology of the Cell 9, no. 2 (1998): 237–47. http://dx.doi.org/10.1091/mbc.9.2.237.

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Recent studies have revealed the expression of multiple putative cytoplasmic dynein heavy chain (DHC) genes in several organisms, with each gene encoding a separate protein isoform. This finding is consistent with the hypothesis that different isoforms do different things, as is the case for the axonemal dyneins. Furthermore, the large number of tasks ascribed to cytoplasmic dynein suggests that there may be additional isoforms not yet identified. Two of the mammalian cytoplasmic dynein heavy chains are DHC1a and DHC1b. DHC1a is conventional cytoplasmic dynein and is found in all organisms exa

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Gusnowski, Eva M., and Martin Srayko. "Visualization of dynein-dependent microtubule gliding at the cell cortex: implications for spindle positioning." Journal of Cell Biology 194, no. 3 (2011): 377–86. http://dx.doi.org/10.1083/jcb.201103128.

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Dynein motors move along the microtubule (MT) lattice in a processive “walking” manner. In the one-cell Caenorhabditis elegans embryo, dynein is required for spindle-pulling forces during mitosis. Posteriorly directed spindle-pulling forces are higher than anteriorly directed forces, and this imbalance results in posterior spindle displacement during anaphase and an asymmetric division. To address how dynein could be asymmetrically activated to achieve posterior spindle displacement, we developed an assay to measure dynein’s activity on individual MTs at the embryo cortex. Our study reveals th

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Bower, Raqual, Kristyn VanderWaal, Eileen O'Toole, et al. "IC138 Defines a Subdomain at the Base of the I1 Dynein That Regulates Microtubule Sliding and Flagellar Motility." Molecular Biology of the Cell 20, no. 13 (2009): 3055–63. http://dx.doi.org/10.1091/mbc.e09-04-0277.

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To understand the mechanisms that regulate the assembly and activity of flagellar dyneins, we focused on the I1 inner arm dynein (dynein f) and a null allele, bop5-2, defective in the gene encoding the IC138 phosphoprotein subunit. I1 dynein assembles in bop5-2 axonemes but lacks at least four subunits: IC138, IC97, LC7b, and flagellar-associated protein (FAP) 120—defining a new I1 subcomplex. Electron microscopy and image averaging revealed a defect at the base of the I1 dynein, in between radial spoke 1 and the outer dynein arms. Microtubule sliding velocities also are reduced. Transformatio

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Hunter, Emily L., Karl Lechtreck, Gang Fu, et al. "The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length." Molecular Biology of the Cell 29, no. 8 (2018): 886–96. http://dx.doi.org/10.1091/mbc.e17-12-0729.

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Axonemal dyneins, including inner dynein arm I1, assemble in the cytoplasm prior to transport into cilia by intraflagellar transport (IFT). How I1 dynein interacts with IFT is not understood. We take advantage of the Chlamydomonas reinhardtii ida3 mutant, which assembles the inner arm I1 dynein complex in the cytoplasm but fails to transport I1 into the cilium, resulting in I1 dynein-deficient axonemes with abnormal motility. The IDA3 gene encodes an ∼115-kDa coiled-coil protein that primarily enters the cilium during ciliary growth but is not an axonemal protein. During growth, IDA3, along wi

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Lin, Jianfeng, Thuc Vy Le, Katherine Augspurger, et al. "FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia." Molecular Biology of the Cell 30, no. 21 (2019): 2659–80. http://dx.doi.org/10.1091/mbc.e19-07-0367.

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Ciliary motility depends on both the precise spatial organization of multiple dynein motors within the 96 nm axonemal repeat and the highly coordinated interactions between different dyneins and regulatory complexes located at the base of the radial spokes. Mutations in genes encoding cytoplasmic assembly factors, intraflagellar transport factors, docking proteins, dynein subunits, and associated regulatory proteins can all lead to defects in dynein assembly and ciliary motility. Significant progress has been made in the identification of dynein subunits and extrinsic factors required for prea

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Liu, Guang, Limei Wang, and Junmin Pan. "Chlamydomonas WDR92 in association with R2TP-like complex and multiple DNAAFs to regulate ciliary dynein preassembly." Journal of Molecular Cell Biology 11, no. 9 (2018): 770–80. http://dx.doi.org/10.1093/jmcb/mjy067.

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Abstract The motility of cilia or eukaryotic flagella is powered by the axonemal dyneins, which are preassembled in the cytoplasm by proteins termed dynein arm assembly factors (DNAAFs) before being transported to and assembled on the ciliary axoneme. Here, we characterize the function of WDR92 in Chlamydomonas. Loss of WDR92, a cytoplasmic protein, in a mutant wdr92 generated by DNA insertional mutagenesis resulted in aflagellate cells or cells with stumpy or short flagella, disappearance of axonemal dynein arms, and diminishment of dynein arm heavy chains in the cytoplasm, suggesting that WD

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Li, M., M. McGrail, M. Serr, and T. S. Hays. "Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte." Journal of Cell Biology 126, no. 6 (1994): 1475–94. http://dx.doi.org/10.1083/jcb.126.6.1475.

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The unidirectional movements of the microtubule-associated motors, dyneins, and kinesins, provide an important mechanism for the positioning of cellular organelles and molecules. An intriguing possibility is that this mechanism may underlie the directed transport and asymmetric positioning of morphogens that influence the development of multicellular embryos. In this report, we characterize the Drosophila gene, Dhc64C, that encodes a cytoplasmic dynein heavy chain polypeptide. The primary structure of the Drosophila cytoplasmic dynein heavy chain polypeptide has been determined by the isolatio

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Porter, M. E., S. Myster, C. Perrone, and E. O'Toole. "Molecular and Structural Studies on Dynein Associated Mutations in Chlamydomonas Flagella." Microscopy and Microanalysis 3, S2 (1997): 219–20. http://dx.doi.org/10.1017/s1431927600007984.

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The dynein ATPases are a large family of motor enzymes that provide the driving force for flagellar motility and contribute to microtubule-based transport inside cells. The challenge for the field is to appreciate the functional significance of the multiple dynein motors, to determine how the cell assembles a motor complex and targets each motor to its appropriate location, and to understand how a cell regulates the activity of each motor to accomplish its specific task(s). In our laboratory, we have capitalized on the highly ordered structural organization of the flagellar axoneme and on the

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Nicholas, Matthew P., Florian Berger, Lu Rao, Sibylle Brenner, Carol Cho, and Arne Gennerich. "Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains." Proceedings of the National Academy of Sciences 112, no. 20 (2015): 6371–76. http://dx.doi.org/10.1073/pnas.1417422112.

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Cytoplasmic dynein is a homodimeric microtubule (MT) motor protein responsible for most MT minus-end–directed motility. Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellular activities) per motor domain (AAA1–4). The main site of ATP hydrolysis, AAA1, is the only site considered by most dynein motility models. However, it remains unclear how ATPase activity and MT binding are coordinated within and between dynein’s motor domains. Using optical tweezers, we characterize the MT-binding strength of recombinant dynein monomers as a function of mechanical tension and nucle

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Sakato-Antoku, Miho, Jeremy L. Balsbaugh, and Stephen M. King. "N-Terminal Processing and Modification of Ciliary Dyneins." Cells 12, no. 20 (2023): 2492. http://dx.doi.org/10.3390/cells12202492.

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Axonemal dyneins are highly complex microtubule motors that power ciliary motility. These multi-subunit enzymes are assembled at dedicated sites within the cytoplasm. At least nineteen cytosolic factors are specifically needed to generate dynein holoenzymes and/or for their trafficking to the growing cilium. Many proteins are subject to N-terminal processing and acetylation, which can generate degrons subject to the AcN-end rule, alter N-terminal electrostatics, generate new binding interfaces, and affect subunit stoichiometry through targeted degradation. Here, we have used mass spectrometry

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Yamamoto, Ryosuke, Masafumi Hirono, and Ritsu Kamiya. "Discrete PIH proteins function in the cytoplasmic preassembly of different subsets of axonemal dyneins." Journal of Cell Biology 190, no. 1 (2010): 65–71. http://dx.doi.org/10.1083/jcb.201002081.

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Axonemal dyneins are preassembled in the cytoplasm before being transported into cilia and flagella. Recently, PF13/KTU, a conserved protein containing a PIH (protein interacting with HSP90) domain, was identified as a protein responsible for dynein preassembly in humans and Chlamydomonas reinhardtii. This protein is involved in the preassembly of outer arm dynein and some inner arm dyneins, possibly as a cofactor of molecular chaperones. However, it is not known which factors function in the preassembly of other inner arm dyneins. Here, we analyzed a novel C. reinhardtii mutant, ida10, and fo

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Piperno, G., and Z. Ramanis. "The proximal portion of Chlamydomonas flagella contains a distinct set of inner dynein arms." Journal of Cell Biology 112, no. 4 (1991): 701–9. http://dx.doi.org/10.1083/jcb.112.4.701.

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A specific type of inner dynein arm is located primarily or exclusively in the proximal portion of Chlamydomonas flagella. This dynein is absent from flagella less than 6 microns long, is assembled during the second half of flagellar regeneration time and is resistant to extraction under conditions causing complete solubilization of two inner arm heavy chains and partial solubilization of three other heavy chains. This and other evidence described in this report suggest that the inner arm row is composed of five distinct types of dynein arms. Therefore, the units of three inner arms that repea

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Li, Shihe, C. Elizabeth Oakley, Guifang Chen, Xiaoyan Han, Berl R. Oakley та Xin Xiang. "Cytoplasmic Dynein's Mitotic Spindle Pole Localization Requires a Functional Anaphase-promoting Complex, γ-Tubulin, and NUDF/LIS1 in Aspergillus nidulans". Molecular Biology of the Cell 16, № 8 (2005): 3591–605. http://dx.doi.org/10.1091/mbc.e04-12-1071.

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In Aspergillus nidulans, cytoplasmic dynein and NUDF/LIS1 are found at the spindle poles during mitosis, but they seem to be targeted to this location via different mechanisms. The spindle pole localization of cytoplasmic dynein requires the function of the anaphase-promoting complex (APC), whereas that of NUDF does not. Moreover, although NUDF's localization to the spindle poles does not require a fully functional dynein motor, the function of NUDF is important for cytoplasmic dynein's targeting to the spindle poles. Interestingly, a γ-tubulin mutation, mipAR63, nearly eliminates the localiza

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Walczak, C. E., and D. L. Nelson. "In vitro phosphorylation of ciliary dyneins by protein kinases from Paramecium." Journal of Cell Science 106, no. 4 (1993): 1369–76. http://dx.doi.org/10.1242/jcs.106.4.1369.

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Paramecium dyneins were tested as substrates for phosphorylation by cAMP-dependent protein kinase, cGMP-dependent protein kinase, and two Ca(2+)-dependent protein kinases that were partially purified from Paramecium extracts. Only cAMP-dependent protein kinase caused significant phosphorylation. The major phosphorylated species was a 29 kDa protein that was present in both 22 S and 12 S dyneins; its phosphate-accepting activity peaked with 22 S dynein. In vitro phosphorylation was maximal at five minutes, then decreased. This decrease in phosphorylation was inhibited by the addition of vanadat

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Ide, Takahiro, Wang Kyaw Twan, Hao Lu, et al. "CFAP53 regulates mammalian cilia-type motility patterns through differential localization and recruitment of axonemal dynein components." PLOS Genetics 16, no. 12 (2020): e1009232. http://dx.doi.org/10.1371/journal.pgen.1009232.

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Motile cilia can beat with distinct patterns, but how motility variations are regulated remain obscure. Here, we have studied the role of the coiled-coil protein CFAP53 in the motility of different cilia-types in the mouse. While node (9+0) cilia of Cfap53 mutants were immotile, tracheal and ependymal (9+2) cilia retained motility, albeit with an altered beat pattern. In node cilia, CFAP53 mainly localized at the base (centriolar satellites), whereas it was also present along the entire axoneme in tracheal cilia. CFAP53 associated tightly with microtubules and interacted with axonemal dyneins

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