The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility

Ina Weisswange, Timothy P. Newsome, Sibylle Schleich and Michael Way ()
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Ina Weisswange: Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3PX, UK
Timothy P. Newsome: Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3PX, UK
Sibylle Schleich: Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3PX, UK
Michael Way: Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3PX, UK

Nature, 2009, vol. 458, issue 7234, 87-91

Abstract: Actin-based motility In recent years there has been much progress in the identification of molecules involved in signalling networks promoting actin-related protein (ARP)2/3-complex-dependent actin polymerization, a reaction that plays an essential role in many cellular processes such as cell migration. A complete molecular understanding how the ARP2/3 complex functions to stimulate actin polymerization requires a detailed knowledge of the organization and dynamics of signalling networks activating this complex. Using live-cell imaging of vaccinia virus-infected cells together with fluorescence bleaching, Weisswange et al. show that the turnover rate of N-WASP, a well known activator of the ARP2/3 complex, is inversely proportional to the rate of actin-based motility of the virus. Actin polymerization is also required to promote N-WASP turnover beneath the virus. These observations are consistent with a model in which the stability of N-WASP association beneath the virus controls the overall rate of ARP2/3-complex-dependent actin-based motility.

Date: 2009
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DOI: 10.1038/nature07773

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