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Dynactin increases the processivity of the cytoplasmic dynein motor

Nature Cell Biology volume 2, pages 20–24 (2000)Cite this article

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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Figure 1: Bead–microtubule-binding probability as a function of the molar ratio of cytoplasmic dynein:beads in the presence of ADP.
Figure 2: Motility characteristics of protein-coated beads in the presence of ATP.
Figure 3: Distributions of the duration of microtubule binding in the presence of ATP.
Figure 4: Effects of antibody incubation on bead motility in the presence of ATP.

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Acknowledgements

We thank members of the Schroer laboratory for valuable discussions; and L. Ehler and the Schroer laboratory for critical reading of the manuscript. This work was supported by grants from the NIH to T.A.S (GM 44589) and to S.J.K. (F32 GM 19061).

Correspondence and requests for materials should be addressed to T.A.S.

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

    Stephen J. King & Trina A. Schroer

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Correspondence to Trina A. Schroer.

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King, S., Schroer, T. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat Cell Biol 2, 20–24 (2000). https://doi.org/10.1038/71338

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