Abstract
A rise in the concentration of cyclic AMP inhibits secretion in human platelets1–3. In mammalian cells the mechanism of action of cyclic AMP involves activation of a protein kinase and results in protein phosphorylation4. It has previously been shown that myosin light chain kinase purified from smooth muscle is a substrate for the catalytic subunit of cyclic AMP-dependent protein kinase5 and that phosphorylation of smooth muscle myosin kinase results in a decrease in its activity6. Here we present evidence that platelet myosin kinase is a substrate for the catalytic subunit of protein kinase and that phosphorylation of this myosin kinase, isolated from a non-muscle cell, decreases the activity of this enzyme. Dephosphorylation of platelet myosin kinase by a purified phosphatase7 restores its original activity. A decrease in myosin kinase activity in platelets would increase the relative amount of unphosphorylated myosin, which unlike phosphorylated myosin, cannot interact with actin8,9. These findings suggest a mechanism by which cyclic AMP might modulate actin–myosin interaction in platelets and other non-muscle cells.
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Hathaway, D., Eaton, C. & Adelstein, R. Regulation of human platelet myosin light chain kinase by the catalytic subunit of cyclic AMP-dependent protein kinase. Nature 291, 252–254 (1981). https://doi.org/10.1038/291252a0
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DOI: https://doi.org/10.1038/291252a0
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