Key result
Actin patch assembly in fission yeast proceeds via two parallel pathways, one dependent on Wsp1p and Vrp1p and another dependent on Myo1p, which converge to activate the Arp2/3 complex.
Offers no immediate clinical applications; extends models of Arp2/3 activation in fission yeast.
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.
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Sirotkin et al. (2005) studied Actin patch assembly in fission yeast. Genetic deletion and fluorescent tagging of nucleation-promoting factors vs. Wild-type yeast strains was evaluated on Actin patch assembly dynamics and biochemical interactions. Actin patch assembly in fission yeast proceeds via two parallel pathways, one dependent on Wsp1p and Vrp1p and another dependent on Myo1p, which converge to activate the Arp2/3 complex.
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