Contraction and polymerization cooperate to assemble and close actomyosin rings around Xenopus oocyte wounds.
Xenopus oocytes assemble an array of F-actin and myosin 2 around plasma membrane wounds. We analyzed this process in living oocytes using confocal time-lapse (four-dimensional) microscopy. Closure of wounds requires assembly and contraction of a classic "contractile ring" composed of F-actin and myosin 2. However, this ring works in concert with a 5-10-microm wide "zone" of localized actin and myosin 2 assembly. The zone forms before the ring and can be uncoupled from the ring by inhibition of cortical flow and contractility. However, contractility and the contractile ring are required for the stability and forward movement of the zone, as revealed by changes in zone dynamics after disruption of contractility and flow, or experimentally induced breakage of the contractile ring. We conclude that wound-induced contractile arrays are provided with their characteristic flexibility, speed, and strength by the combined input of two distinct components: a highly dynamic zone in which myosin 2 and actin preferentially assemble, and a stable contractile actomyosin ring.
Mandato
C A
CA
Department of Zoology, University of Wisconsin, Madison, WI 53706, USA. camandato@facstaff.wisc.edu
Bement
W M
WM
D000199:Actins / Q000502:physiology; D000205:Actomyosin / Q000502:physiology*; D000818:Animals; D002462:Cell Membrane / Q000502:physiology*; D002465:Cell Movement; D003285:Contractile Proteins / Q000502:physiology*; D005260:Female; D009068:Movement / Q000502:physiology*; D009218:Myosins / Q000502:physiology; D009865:Oocytes / Q000502:physiology; D011485:Protein Binding; D011487:Protein Conformation; D014981:Xenopus
D000199:Actins; D003285:Contractile Proteins; D000205:Actomyosin; D009218:Myosins