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)

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 languageEnglish
Pages (from-to)205-208
JournalFEBS Letters
Volume255
DOIs
Publication statusPublished - 11 Sep 1989

Keywords

  • Casein kinase 1
  • Protein kinase C

Fingerprint Dive into the research topics of 'Phosphorylation of protein kinase C by casein kinase-1'. Together they form a unique fingerprint.

  • Cite this

    Vila, J., Walker, J. M., Itarte, E., Weber, M. J., & Sando, J. J. (1989). Phosphorylation of protein kinase C by casein kinase-1. FEBS Letters, 255, 205-208. https://doi.org/10.1016/0014-5793(89)81092-0