Phosphorylation of protein kinase C by casein kinase-1.
Because phosphorylation of protein kinase C (PKC) may provide a mechanism for regulation of this enzyme, we have examined the ability of two other kinases to phosphorylate PKC. Our results show that casein kinase 1 (CK-1), but not casein kinase 2 (CK-2), can phosphorylate PKC in the absence of Ca2+ and phospholipids. The 32P incorporation into PKC in the presence of Ca2+ and phospholipids is also enhanced by CK-1.
Vila
J
J
Department of Microbiology, University of Virginia, Charlottesville 22908.
Walker
J M
JM
Itarte
E
E
Weber
M J
MJ
Sando
J J
JJ
D002118:Calcium / Q000494:pharmacology; D047388:Casein Kinases; D010449:Peptide Mapping; D010743:Phospholipids / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*
D010743:Phospholipids; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C; D002118:Calcium