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Nat Cell Biol. 2000 Jan;2(1):20-4.

Dynactin increases the processivity of the cytoplasmic dynein motor.

Author information

1
Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA.

Abstract

Cytoplasmic dynein supports long-range intracellular movements of cargo in vivo but does not appear to be a processive motor protein by itself. We show here that the dynein activator, dynactin, binds microtubules and increases the average length of cytoplasmic-dynein-driven movements without affecting the velocity or microtubule-stimulated ATPase kinetics of cytoplasmic dynein. Enhancement of microtubule binding and motility by dynactin are both inhibited by an antibody to dynactin's microtubule-binding domain. These results indicate that dynactin acts as a processivity factor for cytoplasmic-dynein-based motility and provide the first evidence that cytoskeletal motor processivity can be affected by extrinsic factors.

PMID:
10620802
DOI:
10.1038/71338
[Indexed for MEDLINE]

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