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Protein kinase C μ selectively activates the mitogen‐activated protein kinase (MAPK) p42 pathway
Author(s) -
Hausser Angelika,
Storz Peter,
Hübner Susanne,
Braendlin Ilona,
Martinez-Moya Marina,
Link Gisela,
Johannes Franz-Josef
Publication year - 2001
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/s0014-5793(01)02219-0
Subject(s) - mitogen activated protein kinase kinase , protein kinase c , map kinase kinase kinase , mapk/erk pathway , cyclin dependent kinase 9 , map2k7 , protein kinase a , microbiology and biotechnology , cyclin dependent kinase 2 , ask1 , c raf , chemistry , kinase , p38 mitogen activated protein kinases , mapk cascade , mitogen activated protein kinase , biology
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.