Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
In resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK 3). These three sites are nested within a single tryptic peptide located just upstream of the basic region...
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Veröffentlicht in: | Cell 1991-02, Vol.64 (3), p.573-584 |
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