Relationship between membrane protein phosphorylation and intracellular translocation of casein kinase in human erythrocytes.
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.
Bordin
L
L
Dipartimento di Chimica Biologica, Università di Padova, Italy.
Clari
G
G
Baggio
B
B
Gambaro
G
G
Moret
V
V
D000255:Adenosine Triphosphate / Q000378:metabolism; D047388:Casein Kinases; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008565:Membrane Proteins / Q000097:blood* / Q000302:isolation & purification; D010750:Phosphoproteins / Q000097:blood* / Q000302:isolation & purification; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011494:Protein Kinases / Q000097:blood*
D008565:Membrane Proteins; D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases