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Science 27 October 2000:
Vol. 290. no. 5492, pp. 801 - 806
DOI: 10.1126/science.290.5492.801
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Reports

Integration of Multiple Signals Through Cooperative Regulation of the N-WASP-Arp2/3 Complex

Kenneth E. Prehoda,12 Jessica A. Scott,12 R. Dyche Mullins,1 Wendell A. Lim12*

The protein N-WASP [a homolog to the Wiskott-Aldrich syndrome protein (WASP)] regulates actin polymerization by stimulating the actin-nucleating activity of the actin-related protein 2/3 (Arp2/3) complex. N-WASP is tightly regulated by multiple signals: Only costimulation by Cdc42 and phosphatidylinositol (4,5)-bisphosphate (PIP2) yields potent polymerization. We found that regulation requires N-WASP's constitutively active output domain (VCA) and two regulatory domains: a Cdc42-binding domain and a previously undescribed PIP2-binding domain. In the absence of stimuli, the regulatory modules together hold the VCA-Arp2/3 complex in an inactive "closed" conformation. In this state, both the Cdc42- and PIP2-binding sites are masked. Binding of either input destabilizes the closed state and enhances binding of the other input. This cooperative activation mechanism shows how combinations of simple binding domains can be used to integrate and amplify coincident signals.

1 Department of Cellular and Molecular Pharmacology, and
2 Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0450, USA.
*   To whom correspondence should be addressed. E-mail: wlim{at}itsa.ucsf.edu

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G. Scita, P. Tenca, L. B. Areces, A. Tocchetti, E. Frittoli, G. Giardina, I. Ponzanelli, P. Sini, M. Innocenti, and P. P. Di Fiore (2001)
J. Cell Biol. 154, 1031-1044
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The Yeast Synaptojanin-like Proteins Control the Cellular Distribution of Phosphatidylinositol (4,5)-Bisphosphate.
C. J. Stefan, A. Audhya, and S. D. Emr (2002)
Mol. Biol. Cell 13, 542-557
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Science. ISSN 0036-8075 (print), 1095-9203 (online)