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Mechanism of autophosphorylation of the multifunctional calcium calmodulin dependent protein kinase



Mechanism of autophosphorylation of the multifunctional calcium calmodulin dependent protein kinase



Journal of Biological Chemistry 260(10): 6427-6433



The multifunctional Ca2+/calmodulin-dependent protein kinase purified from rat brain cytosol undergoes a self-phosphorylation or autophosphorylation reaction. This reaction is autocatalytic. The autophosphorylation reaction and the protein kinase activity toward other substrates are absolutely dependent on the presence of both Ca2+ and calmodulin. Autophosphorylation and phosvitin kinase activity show a similar time course and indistinguishable heat lability. The reaction is a consistent property of every preparation of rat brain kinase. The reaction is present in both crude and highly purified preparations of similar kinases or isozymes from rat lung, spleen, heart, bovine brain and a neuronal tissue from Aplysia californica, a marine mollusk. Phosphorylation of the kinase subunits is not mimicked by addition of cAMP, cGMP, Ca2+ plus diglyceride, or addition of the cAMP-dependent protein kinase, and is not blocked by the heat-stable inhibitor protein of the cAMP-dependent protein kinase. The reaction is intramolecular. Autophosphorylation results in the stoichiometric incorporation of phosphate into both the 51,000- and 60,000-dalton subunits.

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Accession: 005866663

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