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

Malgorzata Boczkowska, Grzegorz Rebowski, David J. Kast and Roberto Dominguez ()
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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

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms4308

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