title: Autoinhibitory and other autoregulatory elements within the dynein motor domain.
abstract: The dyneins are a family of microtubule motor proteins. The motor domain, which represents the C-terminal 2/3 of the dynein heavy chain, exhibits homology to the AAA family of ATPases. It consists of a ring of six related but divergent AAA+ units, with two substantial sized protruding projections, the stem, or tail, which anchors the protein to diverse subcellular sites, and the stalk, which binds microtubules. This article reviews recent efforts to probe the mechanism by which the dyneins produce force, and work from the authors' lab regarding long-range conformational regulation of dynein enzymatic activity.
authors.affiliation: Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, P and S 15-410, 630 W. 168th St., New York, NY 10032, USA. rv2025@columbia.edu
authors.forename: Richard B
authors.initials: RB
authors.lastname: Vallee
authors.forename: Peter
authors.initials: P
authors.lastname: Höök
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D003593:Cytoplasm / Q000378:metabolism; D004398:Dyneins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008868:Microtubule Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D008868:Microtubule Proteins; D020409:Molecular Motor Proteins; D011994:Recombinant Proteins; D004398:Dyneins