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Characterization of two classes of small molecule inhibitors of Arp2/3 complex

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  • B. J. Nolen

    (Department of Molecular Cellular and Developmental Biology,
    Department of Cell Biology,
    Yale University, New Haven, Connecticut 06520, USA
    Present addresses: Department of Chemistry and the Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA (B.J.N.); Kalobios Pharmaceuticals, Inc., South San Francisco, California 94080, USA (N.T.); Five Prime Therapeutics, San Francisco, California 94158, USA (D.W.P.); Gilead Sciences, Inc., Foster City, California 94404, USA (R.S.).)

  • N. Tomasevic

    (Cytokinetics, Inc., South San Francisco, California 94080, USA
    Present addresses: Department of Chemistry and the Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA (B.J.N.); Kalobios Pharmaceuticals, Inc., South San Francisco, California 94080, USA (N.T.); Five Prime Therapeutics, San Francisco, California 94158, USA (D.W.P.); Gilead Sciences, Inc., Foster City, California 94404, USA (R.S.).)

  • A. Russell

    (Cytokinetics, Inc., South San Francisco, California 94080, USA)

  • D. W. Pierce

    (Cytokinetics, Inc., South San Francisco, California 94080, USA
    Present addresses: Department of Chemistry and the Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA (B.J.N.); Kalobios Pharmaceuticals, Inc., South San Francisco, California 94080, USA (N.T.); Five Prime Therapeutics, San Francisco, California 94158, USA (D.W.P.); Gilead Sciences, Inc., Foster City, California 94404, USA (R.S.).)

  • Z. Jia

    (Cytokinetics, Inc., South San Francisco, California 94080, USA)

  • C. D. McCormick

    (Yale University, New Haven, Connecticut 06520, USA)

  • J. Hartman

    (Cytokinetics, Inc., South San Francisco, California 94080, USA)

  • R. Sakowicz

    (Cytokinetics, Inc., South San Francisco, California 94080, USA
    Present addresses: Department of Chemistry and the Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA (B.J.N.); Kalobios Pharmaceuticals, Inc., South San Francisco, California 94080, USA (N.T.); Five Prime Therapeutics, San Francisco, California 94158, USA (D.W.P.); Gilead Sciences, Inc., Foster City, California 94404, USA (R.S.).)

  • T. D. Pollard

    (Department of Molecular Cellular and Developmental Biology,
    Department of Cell Biology,
    Yale University, New Haven, Connecticut 06520, USA)

Abstract

New Arp2/3 complex inhibitors The actin cytoskeleton is dynamic and plays a critical role in several cell biological processes such as cell adhesion, migration and endocytosis. In addition, several pathogens exploit this system to invade and survive within host cells. The Arp2/3 complex nucleates actin filaments and has a unique property to form branched actin networks. In this study, Nolen et al. describe the generation of two types of small molecules that bind to different sites on the Arp2/3 complex and inhibit its actin nucleating activity in vitro and in vivo. These inhibitors provide a powerful approach to study Arp2/3 complex-mediated actin reorganization events in living cells.

Suggested Citation

  • B. J. Nolen & N. Tomasevic & A. Russell & D. W. Pierce & Z. Jia & C. D. McCormick & J. Hartman & R. Sakowicz & T. D. Pollard, 2009. "Characterization of two classes of small molecule inhibitors of Arp2/3 complex," Nature, Nature, vol. 460(7258), pages 1031-1034, August.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7258:d:10.1038_nature08231
    DOI: 10.1038/nature08231
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    Cited by:

    1. Binh An Truong Quang & Ruby Peters & Davide A. D. Cassani & Priyamvada Chugh & Andrew G. Clark & Meghan Agnew & Guillaume Charras & Ewa K. Paluch, 2021. "Extent of myosin penetration within the actin cortex regulates cell surface mechanics," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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