Analysis of phosphorylation and mutation of tyrosine residues of calmodulin on its activation of the erythrocyte Ca(2+)-transporting ATPase.

Abstract excerpt

The role played by the phosphorylation sites of calmodulin on its ability to activate the human erythrocyte Ca(2+)-transporting ATPase (Ca(2+)-ATPase) was evaluated. Phosphorylation of mammalian calmodulin on serine/threonine residues by casein kinase II decreased its affinity for Ca(2+)-ATPase by twofold. In contrast, tyrosine phosphorylation of mammalian calmodulin by the insulin-receptor kinase did not...

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