Phosphorylation of protein kinase C by casein kinase-1

Jordi Vila, Jefrrey M. Walker, Emilio Itarte, Michael J. Weber, Julianne J. Sando

Research output: Contribution to journalArticleResearchpeer-review

11 Citations (Scopus)


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 languageEnglish
Pages (from-to)205-208
JournalFEBS Letters
Publication statusPublished - 11 Sep 1989


  • Casein kinase 1
  • Protein kinase C


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