| Literature DB >> 24015360 |
Benjamin A Smith1, Shae B Padrick, Lynda K Doolittle, Karen Daugherty-Clarke, Ivan R Corrêa, Ming-Qun Xu, Bruce L Goode, Michael K Rosen, Jeff Gelles.
Abstract
During cell locomotion and endocytosis, membrane-tethered WASP proteins stimulate actin filament nucleation by the Arp2/3 complex. This process generates highly branched arrays of filaments that grow toward the membrane to which they are tethered, a conflict that seemingly would restrict filament growth. Using three-color single-molecule imaging in vitro we revealed how the dynamic associations of Arp2/3 complex with mother filament and WASP are temporally coordinated with initiation of daughter filament growth. We found that WASP proteins dissociated from filament-bound Arp2/3 complex prior to new filament growth. Further, mutations that accelerated release of WASP from filament-bound Arp2/3 complex proportionally accelerated branch formation. These data suggest that while WASP promotes formation of pre-nucleation complexes, filament growth cannot occur until it is triggered by WASP release. This provides a mechanism by which membrane-bound WASP proteins can stimulate network growth without restraining it. DOI:http://dx.doi.org/10.7554/eLife.01008.001.Entities:
Keywords: Human; S. cerevisiae; TIRF; WH2; Wiskott-Aldrich syndrome protein; activation; nucleation; verprolin homology
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Year: 2013 PMID: 24015360 PMCID: PMC3762362 DOI: 10.7554/eLife.01008
Source DB: PubMed Journal: Elife ISSN: 2050-084X Impact factor: 8.140