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First published online 12 September 2007
doi: 10.1242/jcs.006049
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Research Article |
1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
2 Van Andel Research Institute, 333 Bostwick Avenue, Grand Rapids, MI 49503, USA
3 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, and Cell Biology and Physiology Center, National Heart, Lung and Blood Institute, Building 50 South Drive, Bethesda, MD 20892-8019, USA
* Author for correspondence (e-mail: watermancm{at}nhlbi.nih.gov)
Accepted 17 July 2007
Cell migration requires spatial and temporal regulation of filamentous actin (F-actin) dynamics. This regulation is achieved by distinct actin-associated proteins, which mediate polymerization, depolymerization, severing, contraction, bundling or engagement to the membrane. Mammalian Diaphanous-related (mDia) formins, which nucleate, processively elongate, and in some cases bundle actin filaments, have been extensively studied in vitro, but their function in the cell has been less well characterized. Here we study the role of mDia2 activity in the dynamic organization of F-actin in migrating epithelial cells. We find that mDia2 localizes in the lamella of migrating epithelial cells, where it is involved in the formation of a stable pool of cortical actin and in maintenance of polymerization-competent free filament barbed ends at focal adhesions. Specific inhibition of mDia2 alters focal adhesion turnover and reduces migration velocity. We suggest that the regulation of filament assembly dynamics at focal adhesions may be necessary for the formation of a stable pool of cortical lamella actin and the proper assembly and disassembly dynamics of focal adhesions, making mDia2 an important factor in epithelial cell migration.
Key words: FRAP, FSM, Adhesion, Depolymerization, Formin
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