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A more recent version of this article appeared on March 1, 2003
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Submitted on August 6, 2002
Revised on November 20, 2002
Accepted on November 25, 2002
1 Dept. of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905
* Corresponding author. E-mail address: mcniven.mark{at}mayo.edu.
The mechanisms by which mammalian cells remodel the actin cytoskeleton in response to motogenic stimuli are complex and a topic of intense study. Dyn2 is a large GTPase that interacts directly with several actin binding proteins, including cortactin. In this study we demonstrate that Dyn2 and cortactin function to mediate dynamic remodeling of the actin cytoskeleton in response to stimulation with the motogenic growth factor PDGF. Upon stimulation, Dyn2 and cortactin co-assemble into large, circular structures on the dorsal cell surface. These "waves" promote an active reorganization of actin filaments in the anterior cytoplasm and function to disassemble actin stress fibers. Importantly, inhibition of Dyn2 and cortactin function potently blocked the formation of waves and subsequent actin reorganization. These findings demonstrate that cortactin and Dyn2 function together in a supramolecular complex that assembles in response to growth factor stimulation and mediates the remodeling of actin to facilitate lamellipodial protrusion at the leading edge of migrating cells.
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