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• W2896095338 abstract "Unlike the WASP family of Arp2/3 complex activators, WISH/DIP/SPIN90 (WDS) family proteins activate actin filament nucleation by the Arp2/3 complex without the need for a preformed actin filament. This allows WDS proteins to initiate branched actin network assembly by providing seed filaments that activate WASP-bound Arp2/3 complex. Despite their important role in actin network initiation, it is unclear how WDS proteins drive the activating steps that require both WASP and pre-existing actin filaments during WASP-mediated nucleation. Here, we show that SPIN90 folds into an armadillo repeat domain that binds a surface of Arp2/3 complex distinct from the two WASP sites, straddling a hinge point that may stimulate movement of the Arp2 subunit into the activated short-pitch conformation. SPIN90 binds a surface on Arp2/3 complex that overlaps with actin filament binding, explaining how it could stimulate the same structural rearrangements in the complex as pre-existing actin filaments. By revealing how WDS proteins activate the Arp2/3 complex, these data provide a molecular foundation to understand initiation of dendritic actin networks and regulation of Arp2/3 complex by its activators." @default.
• W2896095338 created "2018-10-26" @default.
• W2896095338 creator A5040327626 @default.
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• W2896095338 date "2018-10-15" @default.
• W2896095338 modified "2023-10-10" @default.
• W2896095338 title "Structure of the nucleation‐promoting factor <scp>SPIN</scp> 90 bound to the actin filament nucleator Arp2/3 complex" @default.
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• W2896095338 doi "https://doi.org/10.15252/embj.2018100005" @default.
• W2896095338 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6236337" @default.
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• W2896095338 hasPublicationYear "2018" @default.
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