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TitleAbp1 promotes Arp2/3 complex-dependent actin nucleation and stabilizes branch junctions by antagonizing GMF.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 2895, Year 2018
Publish dateJul 24, 2018
AuthorsSiyang Guo / Olga S Sokolova / Johnson Chung / Shae Padrick / Jeff Gelles / Bruce L Goode /
PubMed AbstractFormation 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 ...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.
External linksNat Commun / PubMed:30042427 / PubMed Central
MethodsEM (single particle)
Resolution18.0 - 21.0 Å
Structure data

EMDB-4267:
Arp2/3 complex in open conformation
Method: EM (single particle) / Resolution: 18.0 Å

EMDB-4268:
Abp1-SNAP bound to Arp2/3 complex (class 2)
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-4269:
Abp1-SNAP bound to Arp2/3 complex (class 1)
Method: EM (single particle) / Resolution: 21.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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