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Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs

Author

Listed:
  • Malgorzata Boczkowska

    (Perelman School of Medicine, University of Pennsylvania)

  • Grzegorz Rebowski

    (Perelman School of Medicine, University of Pennsylvania)

  • David J. Kast

    (Perelman School of Medicine, University of Pennsylvania)

  • Roberto Dominguez

    (Perelman School of Medicine, University of Pennsylvania)

Abstract

Actin filament nucleation and branching by Arp2/3 complex is activated by nucleation-promoting factors (NPFs), whose C-terminal WCA region contains binding sites for actin (W) and Arp2/3 complex (CA). It is debated whether one or two NPFs are required for activation. Here we present evidence in support of the two-NPF model and show that actin plays a crucial role in the interactions of two mammalian NPFs, N-WASP and WAVE2, with Arp2/3 complex. Competition between actin–WCA and glia maturation factor (GMF) for binding to Arp2/3 complex suggests that during activation the first actin monomer binds at the barbed end of Arp2. Based on distance constraints obtained by time-resolved fluorescence resonance energy transfer, we define the relative position of the two actin–WCAs on Arp2/3 complex and propose an atomic model of the 11-subunit transitional complex.

Suggested Citation

  • Malgorzata Boczkowska & Grzegorz Rebowski & David J. Kast & Roberto Dominguez, 2014. "Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs," Nature Communications, Nature, vol. 5(1), pages 1-12, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4308
    DOI: 10.1038/ncomms4308
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    Cited by:

    1. Fred E. Fregoso & Malgorzata Boczkowska & Grzegorz Rebowski & Peter J. Carman & Trevor Eeuwen & Roberto Dominguez, 2023. "Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP-family proteins," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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