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. © 1989.
Original language | English |
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Pages (from-to) | 205-208 |
Journal | FEBS Letters |
Volume | 255 |
DOIs | |
Publication status | Published - 11 Sep 1989 |
Keywords
- Casein kinase 1
- Protein kinase C