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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Conserved Sequence
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Cytoplasm / metabolism
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Dyneins / chemistry*
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Dyneins / genetics
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Dyneins / metabolism
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Dyneins / physiology
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Microtubule Proteins / chemistry*
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Microtubule Proteins / genetics
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Microtubule Proteins / metabolism
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Microtubule Proteins / physiology
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Models, Chemical
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Molecular Motor Proteins / chemistry
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Molecular Motor Proteins / genetics
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Molecular Motor Proteins / metabolism
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Molecular Motor Proteins / physiology
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Molecular Sequence Data
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Molecular Weight
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Protein Conformation
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
Substances
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Microtubule Proteins
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Molecular Motor Proteins
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Recombinant Proteins
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Dyneins