Dynactin increases the processivity of the cytoplasmic dynein motor

Nature Cell Biology
S J King, T A Schroer

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.

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Related Concepts

Microtubule-Associated Protein 3
Protoplasm
Motility Proteins
Microtubules
Chick Embryo
Dynein Intermediate Chains
DNA-dependent ATPase
DCTN1
Latex Spheres
Adenosine Triphosphate, Chromium Ammonium Salt

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