Abstract
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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 12:45 p.m.) |
Deposited | 2 years, 1 month ago (July 28, 2023, 10:39 p.m.) |
Indexed | 1 hour, 10 minutes ago (Sept. 2, 2025, 7:36 p.m.) |
Issued | 24 years, 11 months ago (Sept. 18, 2000) |
Published | 24 years, 11 months ago (Sept. 18, 2000) |
Published Online | 24 years, 11 months ago (Sept. 18, 2000) |
Published Print | 24 years, 11 months ago (Sept. 18, 2000) |
@article{Higgs_2000, title={Activation by Cdc42 and Pip2 of Wiskott-Aldrich Syndrome Protein (Wasp) Stimulates Actin Nucleation by Arp2/3 Complex}, volume={150}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.150.6.1311}, DOI={10.1083/jcb.150.6.1311}, number={6}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Higgs, Henry N. and Pollard, Thomas D.}, year={2000}, month=sep, pages={1311–1320} }