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

Max Rodnick-Smith, Su-Ling Liu, Connor J. Balzer, Qing Luan and Brad J. Nolen ()
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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

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: 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.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12226

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DOI: 10.1038/ncomms12226

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