Abp1 promotes Arp2/3 complex-dependent actin nucleation and stabilizes branch junctions by antagonizing GMF

Siyang Guo, Olga S. Sokolova, Johnson Chung, Shae Padrick, Jeff Gelles and Bruce L. Goode ()
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Siyang Guo: Brandeis University
Olga S. Sokolova: Moscow M.V. Lomonosov University
Johnson Chung: Brandeis University
Shae Padrick: Drexel University College of Medicine
Jeff Gelles: Brandeis University
Bruce L. Goode: Brandeis University

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Formation and turnover of branched actin networks underlies cell migration and other essential force-driven processes. Type I nucleation-promoting factors (NPFs) such as WASP recruit actin monomers to Arp2/3 complex to stimulate nucleation. In contrast, mechanisms of type II NPFs such as Abp1 (also known as HIP55 and Drebrin-like protein) are less well understood. Here, we use single-molecule analysis to investigate yeast Abp1 effects on Arp2/3 complex, and find that Abp1 strongly enhances Arp2/3-dependent branch nucleation by stabilizing Arp2/3 on sides of mother filaments. Abp1 binds dynamically to filament sides, with sub-second lifetimes, yet associates stably with branch junctions. Further, we uncover a role for Abp1 in protecting filament junctions from GMF-induced debranching by competing with GMF for Arp2/3 binding. These data, combined with EM structures of Abp1 dimers bound to Arp2/3 complex in two different conformations, expand our mechanistic understanding of type II NPFs.

Date: 2018
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DOI: 10.1038/s41467-018-05260-y

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