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

Angelika Hausser, Peter Storz, Susanne Hübner, Ilona Braendlin, Marina Martinez-Moya, Gisela Link, Franz Josef Johannes

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)39-44
Number of pages6
JournalFEBS Letters
Volume492
Issue number1-2
DOIs
StatePublished - Mar 9 2001

Keywords

  • Mitogen-activated protein kinase
  • Protein kinase C μ
  • Serum response element
  • p42

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Hausser, A., Storz, P., Hübner, S., Braendlin, I., Martinez-Moya, M., Link, G., & Johannes, F. J. (2001). Protein kinase C μ selectively activates the mitogen-activated protein kinase (MAPK) p42 pathway. FEBS Letters, 492(1-2), 39-44. https://doi.org/10.1016/S0014-5793(01)02219-0