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- W2011993897 abstract "Smad proteins are crucial for the intracellular signaling of transforming growth factor-β (TGF-β). Upon their receptor-induced activation, Smad proteins are phosphorylated and translocated to the nucleus to activate the transcription of a select set of target genes. Here, we show that the co-activator p300/CBP bound and acetylated Smad3 as well as Smad2 in vivo, and that the acetylation was stimulated by TGF-β. A major acetylation site of Smad3 by p300/CBP is Lys-378 in the MH2 domain (Smad3C) known to be critical for the regulation of transcriptional activity. Replacement of Lys-378 with Arg decreased the transcriptional activity of GAL4-Smad3C in a luciferase assay. Moreover, p300/CBP potentiated the transcriptional activity of GAL4-Smad3C, but not the acetylation-resistant GAL4-Smad3C(K378R) mutant. These results suggest that acetylation of Smad3 by p300/CBP regulates positively its transcriptional activity." @default.
- W2011993897 created "2016-06-24" @default.
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- W2011993897 date "2006-07-24" @default.
- W2011993897 modified "2023-10-11" @default.
- W2011993897 title "Smad3 is acetylated by p300/CBP to regulate its transactivation activity" @default.
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- W2011993897 doi "https://doi.org/10.1038/sj.onc.1209826" @default.
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