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Originally published In Press as doi:10.1074/jbc.M208739200 on March 11, 2003

J. Biol. Chem., Vol. 278, Issue 20, 17937-17944, May 16, 2003
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Caldesmon Inhibits Arp2/3-mediated Actin Nucleation*

Yoshihiko YamakitaDagger , Fumio Oosawa§, Shigeko YamashiroDagger , and Fumio MatsumuraDagger

From Dagger  Rutgers University, Department of Molecular Biology and Biochemistry, Nelson Laboratories, Busch Campus, Piscataway, New Jersey 08854 and the § Aichi Institute of Technology, Yakusa-cho, Toyota 470-03, Japan

The Arp2/3 complex greatly accelerates actin polymerization, which is thought to play a major role in cell motility by inducing membrane protrusions including ruffling movements. Membrane ruffles contain a variety of actin-binding proteins, which would modulate Arp2/3-dependent actin polymerization. However, their exact roles in actin polymerization remain to be established. Because caldesmon is present in membrane ruffles, as well as in stress fibers, it may alter Arp2/3-mediated actin polymerization. We have found that caldesmon greatly retards Arp2/3-induced actin polymerization. Kinetic analyses have revealed that caldesmon inhibits the nucleation process, whereas it does not largely reduce elongation. Caldesmon is found to inhibit binding of Arp2/3 to F-actin, which apparently reduces the ability of F-actin as a secondary activator of Arp2/3-mediated nucleation. We also have found that the inhibition of the binding between actin and caldesmon either by Ca2+/calmodulin or by phosphorylation with cdc2 kinase reverses the inhibitory effect of caldesmon on Arp2/3-induced actin polymerization. Our results suggest that caldesmon may be a key protein that modulates membrane ruffling and that this may involve changes in caldesmon phosphorylation and/or intracellular calcium concentrations during signal transduction.

* This work was supported by an American Heart Association grant (to S. Y.), a National Institutes of Health grant (to F. M.), and the Busch Memorial Fund.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Member of the New Jersey Cancer Institute.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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