Phosphorylation of myosin light chain and the actin-activated ATPase activity of adrenal medullary myosin.
Myosin light chain kinase was partially purified from bovine adrenal medulla. A polypeptide of Mr 165,000 dalton was identified as kinase by using anti-gizzard myosin light chain kinase IgG on immunoreplica. Phosphorylation of medullary myosin was Ca2+- and calmodulin-dependent. The phosphorylated myosin was showed to enhance the actin-activated Mg2+-ATPase activity. In contrast, the myosin ATPase activity was dramatically decreased by dephosphorylation of myosin.
Kanda
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K
Sobue
K
K
Kakiuchi
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S
D000199:Actins / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000313:Adrenal Medulla / Q000201:enzymology*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology; D002417:Cattle; D004789:Enzyme Activation; D009219:Myosin-Light-Chain Kinase; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification*
D000199:Actins; D002147:Calmodulin; D011494:Protein Kinases; D009219:Myosin-Light-Chain Kinase; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins; D002118:Calcium