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- W2111750583 abstract "Yeast actin patches are dynamic structures that form at the sites of cell growth and are thought to play a role in endocytosis. We used biochemical analysis and live cell imaging to investigate actin patch assembly in fission yeast Schizosaccharomyces pombe. Patch assembly proceeds via two parallel pathways: one dependent on WASp Wsp1p and verprolin Vrp1p converges with another dependent on class 1 myosin Myo1p to activate the actin-related protein 2/3 (Arp2/3) complex. Wsp1p activates Arp2/3 complex via a conventional mechanism, resulting in branched filaments. Myo1p is a weaker Arp2/3 complex activator that makes unstable branches and is enhanced by verprolin. During patch assembly in vivo, Wsp1p and Vrp1p arrive first independent of Myo1p. Arp2/3 complex associates with nascent activator patches over 6-9 s while remaining stationary. After reaching a maximum concentration, Arp2/3 complex patches move centripetally as activator proteins dissociate. Genetic dependencies of patch formation suggest that patch formation involves cross talk between Myo1p and Wsp1p/Vrp1p pathways." @default.
- W2111750583 created "2016-06-24" @default.
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- W2111750583 date "2005-08-08" @default.
- W2111750583 modified "2023-10-16" @default.
- W2111750583 title "Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast" @default.
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- W2111750583 doi "https://doi.org/10.1083/jcb.200502053" @default.
- W2111750583 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2171502" @default.
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