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REGULATION OF MYOSIN LIGHT CHAIN KINASE BY REVERSIBLE PHOSPHORYLATION AND CALCIUM‐CALMODULIN
Author(s) -
Adelstein R. S.,
Conti M. A.,
Pato M. D.
Publication year - 1980
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1980.tb29607.x
Subject(s) - medicine , cardiology
1) Myosin light chain kinases from smooth muscle and platelets can be phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. 2) Phosphorylation of both kinases, in the absence of calmodulin, markedly decreases kinase activity. 3) The decrease in smooth muscle myosin kinase activity is due to a decreased affinity of the phosphorylated kinase for calmodulin. 4) Dephosphorylation of the smooth muscle kinase by a phosphatase isolated from smooth muscle restores the affinity of the kinase for calmodulin.