Abstract
Dynein is a large enzyme complex that has been found in recent years to be responsible for a variety of forms of intracellular movement associated with microtubules. Molecular analysis of several of the polypeptide components of dynein and a related complex has provided important new insight into their structural organization and mechanism of action in the cell.
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Selected References
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- Amos L. A. Kinesin from pig brain studied by electron microscopy. J Cell Sci. 1987 Feb;87(Pt 1):105–111. doi: 10.1242/jcs.87.1.105. [DOI] [PubMed] [Google Scholar]
- Berlin V., Styles C. A., Fink G. R. BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin. J Cell Biol. 1990 Dec;111(6 Pt 1):2573–2586. doi: 10.1083/jcb.111.6.2573. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bloom G. S. Motor proteins for cytoplasmic microtubules. Curr Opin Cell Biol. 1992 Feb;4(1):66–73. doi: 10.1016/0955-0674(92)90060-p. [DOI] [PubMed] [Google Scholar]
- Bloom G. S., Wagner M. C., Pfister K. K., Brady S. T. Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochemistry. 1988 May 3;27(9):3409–3416. doi: 10.1021/bi00409a043. [DOI] [PubMed] [Google Scholar]
- Cheney R. E., Riley M. A., Mooseker M. S. Phylogenetic analysis of the myosin superfamily. Cell Motil Cytoskeleton. 1993;24(4):215–223. doi: 10.1002/cm.970240402. [DOI] [PubMed] [Google Scholar]
- Clark S. W., Meyer D. I. Centractin is an actin homologue associated with the centrosome. Nature. 1992 Sep 17;359(6392):246–250. doi: 10.1038/359246a0. [DOI] [PubMed] [Google Scholar]
- Collins C. A., Vallee R. B. Preparation of microtubules from rat liver and testis: cytoplasmic dynein is a major microtubule associated protein. Cell Motil Cytoskeleton. 1989;14(4):491–500. doi: 10.1002/cm.970140407. [DOI] [PubMed] [Google Scholar]
- Corthésy-Theulaz I., Pauloin A., Pfeffer S. R. Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J Cell Biol. 1992 Sep;118(6):1333–1345. doi: 10.1083/jcb.118.6.1333. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cyr J. L., Pfister K. K., Bloom G. S., Slaughter C. A., Brady S. T. Molecular genetics of kinesin light chains: generation of isoforms by alternative splicing. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10114–10118. doi: 10.1073/pnas.88.22.10114. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Endow S. A., Titus M. A. Genetic approaches to molecular motors. Annu Rev Cell Biol. 1992;8:29–66. doi: 10.1146/annurev.cb.08.110192.000333. [DOI] [PubMed] [Google Scholar]
- Gibbons A. Biotech pipeline: bottleneck ahead. Science. 1991 Oct 18;254(5030):369–370. doi: 10.1126/science.1925590. [DOI] [PubMed] [Google Scholar]
- Gibbons I. R., Gibbons B. H., Mocz G., Asai D. J. Multiple nucleotide-binding sites in the sequence of dynein beta heavy chain. Nature. 1991 Aug 15;352(6336):640–643. doi: 10.1038/352640a0. [DOI] [PubMed] [Google Scholar]
- Gill S. R., Schroer T. A., Szilak I., Steuer E. R., Sheetz M. P., Cleveland D. W. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J Cell Biol. 1991 Dec;115(6):1639–1650. doi: 10.1083/jcb.115.6.1639. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldstein L. S. The kinesin superfamily: tails of functional redundancy. Trends Cell Biol. 1991 Oct;1(4):93–98. doi: 10.1016/0962-8924(91)90036-9. [DOI] [PubMed] [Google Scholar]
- Goodenough U. W., Heuser J. E. Substructure of inner dynein arms, radial spokes, and the central pair/projection complex of cilia and flagella. J Cell Biol. 1985 Jun;100(6):2008–2018. doi: 10.1083/jcb.100.6.2008. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goodson H. V., Spudich J. A. Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequences. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):659–663. doi: 10.1073/pnas.90.2.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hammer J. A. Novel myosins. Trends Cell Biol. 1991 Aug;1(2-3):50–56. doi: 10.1016/0962-8924(91)90089-r. [DOI] [PubMed] [Google Scholar]
- Hirokawa N., Pfister K. K., Yorifuji H., Wagner M. C., Brady S. T., Bloom G. S. Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell. 1989 Mar 10;56(5):867–878. doi: 10.1016/0092-8674(89)90691-0. [DOI] [PubMed] [Google Scholar]
- Holzbaur E. L., Hammarback J. A., Paschal B. M., Kravit N. G., Pfister K. K., Vallee R. B. Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued. Nature. 1991 Jun 13;351(6327):579–583. doi: 10.1038/351579a0. [DOI] [PubMed] [Google Scholar]
- Johnson K. A. Pathway of the microtubule-dynein ATPase and the structure of dynein: a comparison with actomyosin. Annu Rev Biophys Biophys Chem. 1985;14:161–188. doi: 10.1146/annurev.bb.14.060185.001113. [DOI] [PubMed] [Google Scholar]
- Johnson K. A., Wall J. S. Structure and molecular weight of the dynein ATPase. J Cell Biol. 1983 Mar;96(3):669–678. doi: 10.1083/jcb.96.3.669. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kamiya R. Mutations at twelve independent loci result in absence of outer dynein arms in Chylamydomonas reinhardtii. J Cell Biol. 1988 Dec;107(6 Pt 1):2253–2258. doi: 10.1083/jcb.107.6.2253. [DOI] [PMC free article] [PubMed] [Google Scholar]
- King S. M., Wilkerson C. G., Witman G. B. The Mr 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with alpha-tubulin in situ. J Biol Chem. 1991 May 5;266(13):8401–8407. [PubMed] [Google Scholar]
- King S. M., Witman G. B. Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy. J Biol Chem. 1990 Nov 15;265(32):19807–19811. [PubMed] [Google Scholar]
- Koonce M. P., Grissom P. M., McIntosh J. R. Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein. J Cell Biol. 1992 Dec;119(6):1597–1604. doi: 10.1083/jcb.119.6.1597. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kuznetsov S. A., Vaisberg E. A., Shanina N. A., Magretova N. N., Chernyak V. Y., Gelfand V. I. The quaternary structure of bovine brain kinesin. EMBO J. 1988 Feb;7(2):353–356. doi: 10.1002/j.1460-2075.1988.tb02820.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lacey M. L., Haimo L. T. Cytoplasmic dynein is a vesicle protein. J Biol Chem. 1992 Mar 5;267(7):4793–4798. [PubMed] [Google Scholar]
- Lees-Miller J. P., Helfman D. M., Schroer T. A. A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature. 1992 Sep 17;359(6392):244–246. doi: 10.1038/359244a0. [DOI] [PubMed] [Google Scholar]
- Lin S. X., Collins C. A. Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells. J Cell Sci. 1992 Jan;101(Pt 1):125–137. doi: 10.1242/jcs.101.1.125. [DOI] [PubMed] [Google Scholar]
- Lye R. J., Porter M. E., Scholey J. M., McIntosh J. R. Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. Cell. 1987 Oct 23;51(2):309–318. doi: 10.1016/0092-8674(87)90157-7. [DOI] [PubMed] [Google Scholar]
- Mikami A., Paschal B. M., Mazumdar M., Vallee R. B. Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C). Neuron. 1993 May;10(5):787–796. doi: 10.1016/0896-6273(93)90195-w. [DOI] [PubMed] [Google Scholar]
- Mitchell D. R., Kang Y. Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene. J Cell Biol. 1991 May;113(4):835–842. doi: 10.1083/jcb.113.4.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mitchell D. R., Rosenbaum J. L. Protein-protein interactions in the 18S ATPase of Chlamydomonas outer dynein arms. Cell Motil Cytoskeleton. 1986;6(5):510–520. doi: 10.1002/cm.970060510. [DOI] [PubMed] [Google Scholar]
- Ogawa K. Four ATP-binding sites in the midregion of the beta heavy chain of dynein. Nature. 1991 Aug 15;352(6336):643–645. doi: 10.1038/352643a0. [DOI] [PubMed] [Google Scholar]
- Paschal B. M., Mikami A., Pfister K. K., Vallee R. B. Homology of the 74-kD cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function. J Cell Biol. 1992 Sep;118(5):1133–1143. doi: 10.1083/jcb.118.5.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Paschal B. M., Shpetner H. S., Vallee R. B. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol. 1987 Sep;105(3):1273–1282. doi: 10.1083/jcb.105.3.1273. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Paschal B. M., Vallee R. B. Retrograde transport by the microtubule-associated protein MAP 1C. Nature. 1987 Nov 12;330(6144):181–183. doi: 10.1038/330181a0. [DOI] [PubMed] [Google Scholar]
- Pfister K. K., Fay R. B., Witman G. B. Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella. Cell Motil. 1982;2(6):525–547. doi: 10.1002/cm.970020604. [DOI] [PubMed] [Google Scholar]
- Pierre P., Scheel J., Rickard J. E., Kreis T. E. CLIP-170 links endocytic vesicles to microtubules. Cell. 1992 Sep 18;70(6):887–900. doi: 10.1016/0092-8674(92)90240-d. [DOI] [PubMed] [Google Scholar]
- Piperno G., Luck D. J. Axonemal adenosine triphosphatases from flagella of Chlamydomonas reinhardtii. Purification of two dyneins. J Biol Chem. 1979 Apr 25;254(8):3084–3090. [PubMed] [Google Scholar]
- Piperno G., Ramanis Z., Smith E. F., Sale W. S. Three distinct inner dynein arms in Chlamydomonas flagella: molecular composition and location in the axoneme. J Cell Biol. 1990 Feb;110(2):379–389. doi: 10.1083/jcb.110.2.379. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pollard T. D., Doberstein S. K., Zot H. G. Myosin-I. Annu Rev Physiol. 1991;53:653–681. doi: 10.1146/annurev.ph.53.030191.003253. [DOI] [PubMed] [Google Scholar]
- Porter M. E., Johnson K. A. Dynein structure and function. Annu Rev Cell Biol. 1989;5:119–151. doi: 10.1146/annurev.cb.05.110189.001003. [DOI] [PubMed] [Google Scholar]
- Sale W. S., Goodenough U. W., Heuser J. E. The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella. J Cell Biol. 1985 Oct;101(4):1400–1412. doi: 10.1083/jcb.101.4.1400. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schroer T. A., Sheetz M. P. Two activators of microtubule-based vesicle transport. J Cell Biol. 1991 Dec;115(5):1309–1318. doi: 10.1083/jcb.115.5.1309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shimizu T., Johnson K. A. Kinetic evidence for multiple dynein ATPase sites. J Biol Chem. 1983 Nov 25;258(22):13841–13846. [PubMed] [Google Scholar]
- Shpetner H. S., Paschal B. M., Vallee R. B. Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C). J Cell Biol. 1988 Sep;107(3):1001–1009. doi: 10.1083/jcb.107.3.1001. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trueheart J., Boeke J. D., Fink G. R. Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein. Mol Cell Biol. 1987 Jul;7(7):2316–2328. doi: 10.1128/mcb.7.7.2316. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vale R. D., Schnapp B. J., Mitchison T., Steuer E., Reese T. S., Sheetz M. P. Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro. Cell. 1985 Dec;43(3 Pt 2):623–632. doi: 10.1016/0092-8674(85)90234-x. [DOI] [PubMed] [Google Scholar]
- Vallee R. B., Bloom G. S. Mechanisms of fast and slow axonal transport. Annu Rev Neurosci. 1991;14:59–92. doi: 10.1146/annurev.ne.14.030191.000423. [DOI] [PubMed] [Google Scholar]
- Vallee R. B., Wall J. S., Paschal B. M., Shpetner H. S. Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature. 1988 Apr 7;332(6164):561–563. doi: 10.1038/332561a0. [DOI] [PubMed] [Google Scholar]
- Vallee R. Cytoplasmic dynein: advances in microtubule-based motility. Trends Cell Biol. 1991 Jul;1(1):25–29. doi: 10.1016/0962-8924(91)90066-i. [DOI] [PubMed] [Google Scholar]
- Williams B. D., Mitchell D. R., Rosenbaum J. L. Molecular cloning and expression of flagellar radial spoke and dynein genes of Chlamydomonas. J Cell Biol. 1986 Jul;103(1):1–11. doi: 10.1083/jcb.103.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Witman G. B. Axonemal dyneins. Curr Opin Cell Biol. 1992 Feb;4(1):74–79. doi: 10.1016/0955-0674(92)90061-g. [DOI] [PubMed] [Google Scholar]
- Yang J. T., Laymon R. A., Goldstein L. S. A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell. 1989 Mar 10;56(5):879–889. doi: 10.1016/0092-8674(89)90692-2. [DOI] [PubMed] [Google Scholar]
- Yu H., Toyoshima I., Steuer E. R., Sheetz M. P. Kinesin and cytoplasmic dynein binding to brain microsomes. J Biol Chem. 1992 Oct 5;267(28):20457–20464. [PubMed] [Google Scholar]
- Zhang Z., Tanaka Y., Nonaka S., Aizawa H., Kawasaki H., Nakata T., Hirokawa N. The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme. Proc Natl Acad Sci U S A. 1993 Sep 1;90(17):7928–7932. doi: 10.1073/pnas.90.17.7928. [DOI] [PMC free article] [PubMed] [Google Scholar]