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- W2464653460 abstract "The C-terminal of p53 (amino-acids 368-383) represses the DNA binding activity of p53.In vitro,phosphorylation of this region by Protein Kinase C (PKC) is associated with increased DNA binding activity. However, whether PKC can directly modulate p53 functionin vivois not known. Here, we demonstrate that cotransfection of p53 with either PKCα or PKCζ increases p53's transcriptional activity. Mutagenesis of p53 indicates that serine 371 is the major site for phosphorylation by PKCαin vitro.Mutation of serine 371 caused a small decline in p53 activation by PKCα and PKCζ. However, the alternatively spliced murine p53, which lacks the PKC phosphorylation sites, still demonstrated increased transcriptional activation when cotransfected with either PKCα or PKCζ. The results indicate that phosphorylation of p53 by PKCin vitrodoes not correlate with the ability of PKC to upregulate p53's transcriptional activityin vivo." @default.
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- W2464653460 date "1998-04-01" @default.
- W2464653460 modified "2023-09-27" @default.
- W2464653460 title "Regulation of the p53 Protein by Protein Kinase Cα and Protein Kinase Cζ" @default.
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- W2464653460 doi "https://doi.org/10.1006/bbrc.1998.8471" @default.
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