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Science 12 January 1996:
Vol. 271. no. 5246, pp. 207 - 209
DOI: 10.1126/science.271.5246.207
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Reports

Protection Against Osmotic Stress by cGMP-Mediated Myosin Phosphorylation

Hidekazu Kuwayama,  Maria Ecke,  Günther Gerisch,  Peter J. M. Van Haastert (1)

Conventional myosin functions universally as a generator of motive force in eukaryotic cells. Analysis of mutants of the microorganism Dictyostelium discoideum revealed that myosin also provides resistance against high external osmolarities. An osmo-induced increase of intracellular guanosine 3',5'-monophosphate was shown to mediate phosphorylation of three threonine residues on the myosin tail, which caused a relocalization of myosin required to resist osmotic stress. This redistribution of myosin allowed cells to adopt a spherical shape and may provide physical strength to withstand extensive cell shrinkage in high osmolarities.


H. Kuwayama and P. J. M. Van Haastert, Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.
M. Ecke and G. Gerisch, Max-Planck-Institut für Biochemie, D-82143 Martinsried, Germany.
(1) To whom correspondence should be addressed.


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