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Phosphorylation of protein kinase C by casein kinase‐1
Author(s) -
Vila Jordi,
Walker Jefrrey M.,
Itarte Emilio,
Weber Michael J.,
Sando Julianne J.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81092-0
Subject(s) - protein kinase c , casein kinase 1 , casein kinase 2 , phosphorylation , casein kinase 2, alpha 1 , kinase , chemistry , cyclin dependent kinase 2 , mitogen activated protein kinase kinase , biochemistry , protein kinase a , ask1 , cyclin dependent kinase 9 , map2k7 , protein phosphorylation , enzyme , map kinase kinase kinase , microbiology and biotechnology , biology
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 Ca 2+ and phospholipids. The 32 P incorporation into PKC in the presence of Ca 2+ and phospholipids is also enhanced by CK‐1.