Protein kinase C μ selectively activates the mitogen‐activated protein kinase (MAPK) p42 pathway

FEBS Letters

Hübner, Susanne¹  Hausser, Angelika³  Martinez-Moya, Marina¹  Link, Gisela³  Storz, Peter²  Braendlin, Ilona¹  Johannes, Franz-Josef¹ 

[1] Fraunhofer Institute for Interfacial Engineering and Biotechnology, Nobelstraße 12, 70569 Stuttgart, Germany;Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA;Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany

关键词: Protein kinase C μ;    Mitogen-activated protein kinase;    p42;    Serum response element;   

DOI  :  10.1016/S0014-5793(01)02219-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Here we show that human protein kinase C μ (PKCμ) activates the mitogen-activated protein kinase (MAPK). Transient expression of constitutive active PKCμ leads to an activation of Raf-1 kinase as demonstrated by in vitro phosphorylation of MAPK. PKCμ enhances transcriptional activity of a basal thymidine kinase promotor containing serum response elements (SREs) as shown by luciferase reporter gene assays. SRE driven gene activation by PKCμ is triggered by the Elk-1 ternary complex factor. PKCμ-mediated activation of SRE driven transcription can be inhibited by the MEK1 inhibitor PD98059. In contrast to the activation of the p42/ERK1 MAPK cascade, transient expression of constitutive active PKCμ does neither affect c-jun N-terminal kinase nor p38 MAPK.

【 授权许可】

Unknown