Hausser, A.A.HausserStorz, P.P.StorzHübner, S.S.HübnerBrändlin, I.I.BrändlinMartinez-Moya, M.M.Martinez-MoyaLink, G.G.LinkJohannes, F.J.F.J.Johannes2022-03-032022-03-032001https://publica.fraunhofer.de/handle/publica/19911510.1016/S0014-5793(01)02219-0Here we show that human protein kinase C mu (PKC mu) activates the mitogen-activated protein kinase (MAPK). Transient expression of constitutive active PKC mu leads to an activation of Raf-1 kinase as demonstrated by in vitro phosphorylation of MAPK. PKC mu 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 PKC mu is triggered by the Elk-1 ternary complex factor. PKC mu-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 PKC mu does neither affect c-jun N-terminal kinase nor p38 MAPK.en610620660572Protein kinase C µ selectively activates the mitogen-activated protein kinase (MAPK) p42 pathwayjournal article