ArticleProtein science : a publication of the Protein Society2002
Subunit organization in cytoplasmic dynein subcomplexes.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 87 citations in OpenAlex.
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Dync1li1 is required for the survival of mammalian cochlear hair cells by regulating the transportation of autophagosomes.PLoS genetics · 2022Article
- DYNC1LI2 regulates localization of the chaperone-mediated autophagy receptor LAMP2A and improves cellular homeostasis in cystinosis.Autophagy · 2022Article
- km23-1/DYNLRB1 regulation of MEK/ERK signaling and R-Ras in invasive human colorectal cancer cells.Cell biology international · 2020Article
- DnaJB6 is a RanGTP-regulated protein required for microtubule organization during mitosis.Journal of cell science · 2019Article
- A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport.PLoS biology · 2019Article
- Article
- The Light Intermediate Chain 2 Subpopulation of Dynein Regulates Mitotic Spindle Orientation.Scientific reports · 2016Article
- Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.Cytoskeleton (Hoboken, N.J.) · 2015Review
- Dynein light intermediate chains maintain spindle bipolarity by functioning in centriole cohesion.The Journal of cell biology · 2014Article
- A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region.eLife · 2014Article
- Reduced pachytene piRNAs and translation underlie spermiogenic arrest in Maelstrom mutant mice.The EMBO journal · 2014Article
- In vitro reconstitution of a highly processive recombinant human dynein complex.The EMBO journal · 2014Article
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
- A dynein motor attachment complex regulates TGFß/Smad3 signaling.International journal of biological sciences · 2013Article
- Reconstitution of the human cytoplasmic dynein complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.Molecular biology of the cell · 2012Article
- Ndel1-derived peptides modulate bidirectional transport of injected beads in the squid giant axon.Biology open · 2012Article
- Multiple modes of cytoplasmic dynein regulation.Nature cell biology · 2012Article
- A role for Tctex-1 (DYNLT1) in controlling primary cilium length.European journal of cell biology · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Because cytoplasmic dynein plays numerous critical roles in eukaryotic cells, determining the subunit composition and the organization and functions of the subunits within dynein are important goals. This has been difficult partly because of accessory polypeptide heterogeneity of dynein populations. The motor domain containing heavy chains of cytoplasmic dynein are associated with multiple intermediate, light intermediate, and light chain accessory polypeptides. We examined the organization of these subunits within cytoplasmic dynein by separating the molecule into two distinct subcomplexes. These subcomplexes were competent to reassemble into a molecule with dynein-like properties. One subcomplex was composed of the dynein heavy and light intermediate chains whereas the other subcomplex was composed of the intermediate and light chains. The intermediate and light chain subcomplex could be further separated into two pools, only one of which contained dynein light chains. The two pools had distinct intermediate chain compositions, suggesting that intermediate chain isoforms have different light chain-binding properties. When the two intermediate chain pools were characterized by analytical velocity sedimentation, at least four molecular components were seen: intermediate chain monomers, intermediate chain dimers, intermediate chain monomers with bound light chains, and a mixture of intermediate chain dimers with assorted bound light chains. These data provide new insights into the compositional heterogeneity and assembly of the cytoplasmic dynein complex and suggest that individual dynein molecules have distinct molecular compositions in vivo.
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