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doi: 10.1242/10.1242/dev.00298

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Development 130, 671-681 (2003)
Copyright © 2003 The Company of Biologists Limited

Roles of myosin phosphatase during Drosophila development

Change Tan1, Beth Stronach1 and Norbert Perrimon1,2,*

1 Department of Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
2 Howard Hughes Medical Institute, 200 Longwood Avenue, Boston, MA 02115, USA

* Author for correspondence (e-mail: perrimon{at}rascal.med.harvard.edu)

Accepted 21 November 2002

Myosins are a superfamily of actin-dependent molecular motor proteins, among which the bipolar filament forming myosins II have been the most studied. The activity of smooth muscle/non-muscle myosin II is regulated by phosphorylation of the regulatory light chains, that in turn is modulated by the antagonistic activity of myosin light chain kinase and myosin light chain phosphatase. The phosphatase activity is mainly regulated through phosphorylation of its myosin binding subunit MYPT. To identify the function of these phosphorylation events, we have molecularly characterized the Drosophila homologue of MYPT, and analyzed its mutant phenotypes. We find that Drosophila MYPT is required for cell sheet movement during dorsal closure, morphogenesis of the eye, and ring canal growth during oogenesis. Our results indicate that the regulation of the phosphorylation of myosin regulatory light chains, or dynamic activation and inactivation of myosin II, is essential for its various functions during many developmental processes.

Key words: Rac, Rho, Rho kinase, Myosin II, Myosin phosphatase, zipper, spaghetti-squash, MYPT, Dorsal closure, Ring canal growth, Eye morphogenesis, Drosophila melanogaster


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