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 language | English (US) |
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Pages (from-to) | 39-44 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 492 |
Issue number | 1-2 |
DOIs | |
State | Published - 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