Activation by Cdc42 and PIP2 of Wiskott-Aldrich Syndrome protein (WASp) Stimulates Actin Nucleation by Arp2/3 Complex

doi:10.1083/jcb.150.6.1311

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Published online 18 September 2000. doi:10.1083/jcb.150.6.1311

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© The Rockefeller University Press, 0021-9525/2000/9/1311/ $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. Higgs^a and Thomas D. Pollard^a
^a The Salk Institute for Biological Studies, La Jolla, California 92037

Correspondence to: 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) frombovine thymus and studied its ability to stimulate actin nucleationby Arp2/3 complex. WASp alone is inactive in the presence orabsence of 0.5 µM GTP-Cdc42. Phosphatidylinositol 4,5bisphosphate (PIP₂) micelles allowed WASp to activate actinnucleation by Arp2/3 complex, and this was further enhancedtwofold by GTP-Cdc42. Filaments nucleated by Arp2/3 complexand WASp in the presence of PIP₂ and Cdc42 concentrated aroundlipid micelles and vesicles, providing that Cdc42 was GTP-boundand prenylated. Thus, the high concentration of WASp in neutrophils(9 µM) is dependent on interactions with both acidic lipidsand GTP-Cdc42 to activate actin nucleation by Arp2/3 complex.The results also suggest that membrane binding increases thelocal concentrations of Cdc42 and WASp, favoring their interaction.

Key Words: prenylation, membrane, GBD, neutrophil, thymus

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