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Published online January 2, 2007
doi:10.1083/jcb.200609116
The Journal of Cell Biology, Vol. 176, No. 1, 27-33
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Tamada et al.
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 Two distinct modes of myosin assembly and dynamics during epithelial wound closure

Masako Tamada1, Tomas D. Perez2, W. James Nelson2, and Michael P. Sheetz1

1 Department of Biological Sciences, Columbia University, New York, NY 10027
2 Department of Biological Sciences and Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305

Correspondence to Michael P. Sheetz: ms2001{at}columbia.edu

Actomyosin contraction powers the sealing of epithelial sheets during embryogenesis and wound closure; however, the mechanisms are poorly understood. After laser ablation wounding of Madin–Darby canine kidney cell monolayers, we observed distinct steps in wound closure from time-lapse images of myosin distribution during resealing. Immediately upon wounding, actin and myosin II regulatory light chain accumulated at two locations: (1) in a ring adjacent to the tight junction that circumscribed the wound and (2) in fibers at the base of the cell in membranes extending over the wound site. Rho-kinase activity was required for assembly of the myosin ring, and myosin II activity was required for contraction but not for basal membrane extension. As it contracted, the myosin ring moved toward the basal membrane with ZO-1 and Rho-kinase. Thus, we suggest that tight junctions serve as attachment points for the actomyosin ring during wound closure and that Rho-kinase is required for localization and activation of the contractile ring.

M. Tamada's present address is Kobe University Graduate School of Medicine, Chuo-ku, Kobe 650-0017 Hyogo, Japan.

T.D. Perez's present address is Department of Biological Sciences, Columbia University, New York, NY 10027.

Abbreviation used in this paper: MLC, myosin II regulatory light chain.


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