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

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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
    Present address: School of Molecular and Microbial Biosciences, G08 - Biochemistry and Microbiology, University of Sydney, New South Wales 2006, Australia.)

  • 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)

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.

Suggested Citation

  • Ina Weisswange & Timothy P. Newsome & Sibylle Schleich & Michael Way, 2009. "The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility," Nature, Nature, vol. 458(7234), pages 87-91, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7234:d:10.1038_nature07773
    DOI: 10.1038/nature07773
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    Cited by:

    1. Yiqi Huang & Valter Bergant & Vincent Grass & Quirin Emslander & M. Sabri Hamad & Philipp Hubel & Julia Mergner & Antonio Piras & Karsten Krey & Alexander Henrici & Rupert Öllinger & Yonas M. Tesfamar, 2024. "Multi-omics characterization of the monkeypox virus infection," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

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