title: Phosphorylation of protein kinase C by casein kinase-1.
abstract: 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.
authors: Department of Microbiology, University of Virginia, Charlottesville 22908.
authors: J
authors: J
authors: Vila
authors: J M
authors: JM
authors: Walker
authors: E
authors: E
authors: Itarte
authors: M J
authors: MJ
authors: Weber
authors: J J
authors: JJ
authors: Sando
mesh_terms: 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*
chemical_list: D010743:Phospholipids; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C; D002118:Calcium