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MBC in Press, published online ahead of print March 14, 2007
Mol. Biol. Cell 10.1091/mbc.E06-08-0695

A more recent version of this article appeared on June 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E06-08-0695 on March 21, 2007
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Submitted on August 11, 2006
Revised on February 9, 2007
Accepted on March 2, 2007

Dynactin Is Required for Coordinated Bidirectional Motility, but Not for Dynein Membrane Attachment

Marjan Haghnia,*{dagger} Valeria Cavalli,*{dagger} Sameer B. Shah,* Kristina Schimmelpfeng,* Richard Brusch,* Ge Yang,{ddagger} Cheryl Herrera,* Aaron Pilling,{sect} and Lawrence S.B. Goldstein*

*Howard Hughes Medical Institute and Department of Cellular and Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, CA 92093-0683; {ddagger}Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037; {sect}Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104

Monitoring Editor: Yixian Zheng

Transport of cellular and neuronal vesicles, organelles, and other particles along microtubules requires the molecular motor protein dynein (Mallik and Gross, 2004). Critical to dynein function is dynactin, a multi-protein complex commonly thought to be required for dynein attachment to membrane compartments (Karki and Holzbaur, 1999). Recent work has also found that mutations in dynactin can cause the human motor neuron disease, ALS (Puls et al., 2003). Thus, it is essential to understand the in vivo function of dynactin. To test directly and rigorously the hypothesis that dynactin is required to attach dynein to membranes, we used both a Drosophila mutant and RNA interference to generate organisms and cells lacking the critical dynactin subunit Arp1. Contrary to expectation, we found that apparently normal amounts of dynein associate with membrane compartments in the absence of a fully assembled dynactin complex. In addition, anterograde and retrograde organelle movement in dynactin deficient axons was completely disrupted, resulting in substantial changes in vesicle kinematic properties. Although effects on retrograde transport are predicted by the proposed function of dynactin as a regulator of dynein processivity, the additional effects we observed on anterograde transport also suggest potential roles for dynactin in mediating kinesin-driven transport and in coordinating the activity of opposing motors (King and Schroer, 2000).

{dagger}These authors contributed equally to this work.

Address correspondence to: Lawrence S.B. Goldstein (lgoldstein{at}ucsd.edu)




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