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

Nat Commun. 2018 Jul 24;9(1):2895
Siyang Guo 1 , Olga S Sokolova 2 , Johnson Chung 3 , Shae Padrick 4 , Jeff Gelles 3 , Bruce L Goode 5
Siyang Guo 1 , Olga S Sokolova 2 , Johnson Chung 3 , Shae Padrick 4 , Jeff Gelles 3 , Bruce L Goode 5
+ et al

[No authors listed]

Author information
  • 1 Department of Biology, Brandeis University, Waltham, MA, 02454, USA.
  • 2 Department of Biology, Moscow M.V. Lomonosov University, Moscow, 119234, Russia.
  • 3 Department of Biochemistry, Brandeis University, Waltham, MA, 02454, USA.
  • 4 Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, 19102, USA.
  • 5 Department of Biology, Brandeis University, Waltham, MA, 02454, USA. goode@brandeis.edu.

摘要


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.