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Myosin and actin
Regulation of the interaction between smooth muscle myosin and actin
KATHLEEN M. TRYBUS, DAVID M. WARSHAW
J Cell Sci 1991 1991: 87-89; doi: 10.1242/jcs.1991.Supplement_14.18
KATHLEEN M. TRYBUS
Rosenstiel Research Center, Brandeis University, Waltham, MA 02254, USA
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DAVID M. WARSHAW
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Summary

Phosphorylation of the regulatory light chain of smooth muscle myosin efficiently regulates the actin-activated ATPase activity of myosin filaments in solution and actin movement in an in vitro motility assay, independently of thin-filament regulatory proteins. Filaments containing both phosphorylated and dephosphorylated heads move actin at intermediate rates, depending on the relative proportions of the two myosin species. The decrease in velocity can be accounted for by mechanical interaction; between phosphorylated heads and ‘weak-binding’ dephosphorylated crossbridges. These results imply that shortening velocity could be modulated in any muscle by varying the relative proportions of two populations of crossbridges with different cycling rates.

  • © The Company of Biologists Limited 1991
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Keywords

  • smooth muscle myosin
  • light chain phosphorylation
  • motility assay

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Regulation of the interaction between smooth muscle myosin and actin
KATHLEEN M. TRYBUS, DAVID M. WARSHAW
J Cell Sci 1991 1991: 87-89; doi: 10.1242/jcs.1991.Supplement_14.18
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Regulation of the interaction between smooth muscle myosin and actin
KATHLEEN M. TRYBUS, DAVID M. WARSHAW
J Cell Sci 1991 1991: 87-89; doi: 10.1242/jcs.1991.Supplement_14.18

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