title: The molecular anatomy of dynein.
abstract: Recent molecular, genetic and functional studies have led to an unparalleled growth in our understanding of dynein and the roles played by the various polypeptides of these massive macromolecular assemblies. Dyneins are highly complex 1-2MDa complexes that function as molecular motor and move the cargo to which they are attached towards the minus-end of a microtubule. Dynein motor function is a property of the heavy chains, whereas the intermediate chains are involved in attachment to the appropriate cargo. In order for useful work to be obtained, motor and cargo-binding activities must be tightly controlled. Current data suggest that this is the role played by certain accessory light-chain proteins. The LC8 is highly conserved and found in many enzyme systems. This protein is essential in multicellular organisms. The dynein light chains Tctex1 and Tctex2 have been implicated in the non-Mendelian transmission of variant forms of mouse chromosome 17.
authors.affiliation: Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06032-3305, USA.
authors.forename: A
authors.initials: A
authors.lastname: Harrison
authors.forename: S M
authors.initials: SM
authors.lastname: King
mesh_terms: D000818:Animals; D002465:Cell Movement; D004398:Dyneins / Q000502:physiology*; D006801:Humans; D020409:Molecular Motor Proteins / Q000502:physiology*; D011487:Protein Conformation
chemical_list: D020409:Molecular Motor Proteins; D004398:Dyneins