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Vol. 14, Issue 3, 1085-1096, March 2003
Department of Biochemistry and Molecular Biology, Mayo
Clinic, Rochester, Minnesota 55905
The mechanisms by which mammalian cells remodel the actin
cytoskeleton in response to motogenic stimuli are complex and a topic
of intense study. Dynamin 2 (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 platelet-derived growth factor.
On stimulation, Dyn2 and cortactin coassemble 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.
Online version of this article contains video material for some
figures. Online version available at www.molbiolcell.org.
*
These authors contributed equally to this study.
Corresponding author. E-mail address:
mcniven.mark{at}mayo.edu.
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