The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the okadaic acid (strong inhibitor of P-Ser/Thr-protein phosphatase(s)), is accompanied by a release of casein kinase from the membrane into cytosol. Such an intracellular translocation might provide a feedback mechanism for the regulation of the casein kinase catalyzed phosphorylation of membrane proteins in the human erythrocytes. (C) 1994 Academic Press, Inc.
Relationship Between Membrane-protein Phosphorylation and Intracellular Translocation of Casein Kinase In Human Erythrocytes
BORDIN, LUCIANA;CLARI, GIULIO;BAGGIO, BRUNO;MORET, VITTORIO
1994
Abstract
The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the okadaic acid (strong inhibitor of P-Ser/Thr-protein phosphatase(s)), is accompanied by a release of casein kinase from the membrane into cytosol. Such an intracellular translocation might provide a feedback mechanism for the regulation of the casein kinase catalyzed phosphorylation of membrane proteins in the human erythrocytes. (C) 1994 Academic Press, Inc.
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