Reference - PMID:16087707 - Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast.
Reference summary
- PubMed ID
- PMID:16087707
- Title
- Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast.
- Authors
- Sirotkin V, Beltzner CC, Marchand JB, Pollard TD
- Citation
- J Cell Biol 2005 Aug 15;170(4):637-48
- Publication year
- 2005
- 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.
