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J. Cell Biol. 150 (6): 1311-1320

Copyright © 2000 by the Rockefeller University Press.

© The Rockefeller University Press, /2000/9/1311/ $5.00
The Journal of Cell Biology, Volume 150, Number 6, September 18, 2000 1311-1320
Original Article Activation by Cdc42 and PIP2 of Wiskott-Aldrich Syndrome protein (WASp) Stimulates Actin Nucleation by Arp2/3 Complex Henry N. Higgsa and Thomas D. Pollarda a The Salk Institute for Biological Studies, La Jolla, California 92037 Thomas D. Pollard, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037. Tel:(858) 453-4100 x1716 Fax:(858) 452-3683

We purified native WASp (Wiskott-Aldrich Syndrome protein) from bovine thymus and studied its ability to stimulate actin nucleation by Arp2/3 complex. WASp alone is inactive in the presence or absence of 0.5 µM GTP-Cdc42. Phosphatidylinositol 4,5 bisphosphate (PIP2) micelles allowed WASp to activate actin nucleation by Arp2/3 complex, and this was further enhanced twofold by GTP-Cdc42. Filaments nucleated by Arp2/3 complex and WASp in the presence of PIP2 and Cdc42 concentrated around lipid micelles and vesicles, providing that Cdc42 was GTP-bound and prenylated. Thus, the high concentration of WASp in neutrophils (9 µM) is dependent on interactions with both acidic lipids and GTP-Cdc42 to activate actin nucleation by Arp2/3 complex. The results also suggest that membrane binding increases the local concentrations of Cdc42 and WASp, favoring their interaction.

prenylation, membrane, GBD, neutrophil, thymus

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