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• W2149446912 startingPage "333" @default.
• W2149446912 abstract "We reported previously that activation of endogenous activator protein 1 (AP-1) in chicken embryo fibroblasts is essential for the cellular transformation induced by v-src, and we further showed that the activation of AP-1 is accompanied by elevation of Fra-2 and c-Jun expression and also high-level phosphorylation of Fra-2 by activated endogenous extracellular signal-regulated kinase [mitogen-activated protein kinase (MAPK)]. Here, we report that the transcriptional activity of Fra-2/c-Jun heterodimer was greatly enhanced by cotransfecting a constitutively active mutant of MEK1 gene (MEK-DD) into F9 cells, indicating that Fra-2 was converted into an active transactivator after phosphorylation by MAPK. High-level expression of MEK-DD alone was sufficient to induce clear cellular transformation of chicken embryo fibroblasts, which caused constitutive activation of endogenous MAPK, hyperphosphorylation of Fra-2, and elevation of fra-2 and c-jun gene expression. These results indicate that phosphorylation of Fra-2 by MAPK plays an important role in stimulating endogenous AP-1 activity in a positive autoregulation mechanism, in which phosphorylated Fra-2 induces fra-2 expression through AP-1 binding sites present in its promoter. We also localized the Fra-2 phosphorylation sites by MAPK to three threonine and three serine residues in the COOH-terminal region by means of site-directed mutagenesis and showed that the threonine residues were more susceptible to MAPK." @default.
• W2149446912 created "2016-06-24" @default.
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• W2149446912 date "1999-05-01" @default.
• W2149446912 modified "2023-10-12" @default.
• W2149446912 title "Fra-2-positive autoregulatory loop triggered by mitogen-activated protein kinase (MAPK) and Fra-2 phosphorylation sites by MAPK." @default.
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• W2149446912 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10359014" @default.
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