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Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex

Author

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  • Max Rodnick-Smith

    (University of Oregon)

  • Su-Ling Liu

    (Institute of Molecular Biology, University of Oregon)

  • Connor J. Balzer

    (University of Oregon)

  • Qing Luan

    (Institute of Molecular Biology, University of Oregon)

  • Brad J. Nolen

    (University of Oregon)

Abstract

Nucleation of branched actin filaments by Arp2/3 complex is tightly regulated to control actin assembly in cells. Arp2/3 complex activation involves conformational changes brought about by ATP, Nucleation Promoting Factor (NPF) proteins, actin filaments and NPF-recruited actin monomers. To understand how these factors promote activation, we must first understand how the complex is held inactive in their absence. Here we demonstrate that the Arp3 C-terminal tail is a structural switch that prevents Arp2/3 complex from adopting an active conformation. The interaction between the tail and a hydrophobic groove in Arp3 blocks movement of Arp2 and Arp3 into an activated filament-like (short pitch) conformation. Our data indicate ATP binding destabilizes this interaction via an allosteric link between the Arp3 nucleotide cleft and the hydrophobic groove, thereby promoting the short-pitch conformation. Our results help explain how Arp2/3 complex is locked in an inactive state without activators and how autoinhibition is relieved.

Suggested Citation

  • Max Rodnick-Smith & Su-Ling Liu & Connor J. Balzer & Qing Luan & Brad J. Nolen, 2016. "Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex," Nature Communications, Nature, vol. 7(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12226
    DOI: 10.1038/ncomms12226
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