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Published online 13 August 2001. doi:10.1083/jcb.200103105
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© The Rockefeller University Press, 0021-9525/2001/8/785 $5.00
The Journal of Cell Biology, Volume 154, Number 4, August 20, 2001 785-798

Article

Contraction and polymerization cooperate to assemble and close actomyosin rings around Xenopus oocyte wounds



Craig A. Mandato1 and William M. Bement1,2

1 Department of Zoology, University of Wisconsin, Madison, WI 53706
2 Program in Cellular and Molecular Biology, University of Wisconsin, Madison, WI 53706

Address correspondence to Craig A. Mandato, Department of Zoology, University of Wisconsin, 1117 West Johnson St., Madison, WI 53706. Tel.: (608) 262-5683. Fax: (608) 262-9083. E-mail: camandato{at}facstaff.wisc.edu

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-µm 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.

Key Words: wound healing; cytokinesis; actin polymerization; dorsal closure; myosin polymerization


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