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Vol. 17, Issue 3, 1354-1363, March 2006
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Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110
Submitted October 7, 2005;
Revised December 8, 2005;
Accepted December 27, 2005
Monitoring Editor: Sandra Schmid
Actin assembly nucleated by Arp2/3 complex has been implicated in the formation and movement of endocytic vesicles. The dendritic nucleation model has been proposed to account for Arp2/3-mediated actin assembly and movement. Here, we explored the model by examining the role of capping protein in vivo, with quantitative tracking analysis of fluorescence markers for different stages of endocytosis in yeast. Capping protein was most important for the initial movement of endocytic vesicles away from the plasma membrane, which presumably corresponds to vesicle scission and release. The next phase of endosome movement away from the plasma membrane was also affected, but less so. The results are consistent with the dendritic nucleation model's prediction of capping protein as important for efficient actin assembly and force production. In contrast, the movement of late-stage endocytic vesicles, traveling through the cytoplasm en route to the vacuole, did not depend on capping protein. The movement of these vesicles was found previously to depend on Lsb6, a WASp interactor, whereas Lsb6 was found here to be dispensable for early endosome movement. Thus, the molecular requirements for Arp2/3-based actin assembly differ in early versus later stages of endocytosis. Finally, acute loss of actin cables led to increased patch motility.
Abbreviations used: CP, capping protein; LatA, latrunculin A; MSD, mean squared displacement.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
* These authors contributed equally to this work.
Present address: Department of Biology, Missouri State University, Springfield, MO 65897.
Address correspondence to: John A. Cooper (jcooper{at}wustl.edu).
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