Phosphorylation of protein kinase C by casein kinase-1

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

doi:https://doi.org/10.1016/0014-5793(89)81092-0

Phosphorylation of protein kinase C by casein kinase-1

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

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-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 language	English
Pages (from-to)	205-208
Journal	FEBS Letters
Volume	255
DOIs	https://doi.org/10.1016/0014-5793(89)81092-0
Publication status	Published - 11 Sep 1989

Keywords

Casein kinase 1
Protein kinase C

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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

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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. {\textcopyright} 1989.",

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AU - Vila, Jordi

AU - Walker, Jefrrey M.

AU - Itarte, Emilio

AU - Weber, Michael J.

AU - Sando, Julianne J.

PY - 1989/9/11

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N2 - 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.

AB - 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.

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KW - Protein kinase C

U2 - https://doi.org/10.1016/0014-5793(89)81092-0

DO - https://doi.org/10.1016/0014-5793(89)81092-0

M3 - Article

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