PubMed:10367897 JSONTXT

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":115},"obj":"Sentence"},{"id":"S2","span":{"begin":116,"end":230},"obj":"Sentence"},{"id":"S3","span":{"begin":231,"end":393},"obj":"Sentence"},{"id":"S4","span":{"begin":394,"end":562},"obj":"Sentence"},{"id":"S5","span":{"begin":563,"end":776},"obj":"Sentence"},{"id":"S6","span":{"begin":777,"end":990},"obj":"Sentence"}],"text":"CBP/p300 integrates Raf/Rac-signaling pathways in the transcriptional induction of NF-ATc during T cell activation.\nNF-ATc, an inducibly expressed transcription factor, controls gene expression in T lymphocytes and cardiomyocytes. We show here that the transcriptional co-activators CBP/p300 bind to and control the activity of the inducible N-terminal transactivation domain of NF-ATc, TAD-A. Similar to the N terminal transactivation domain of c-Jun, TAD-A is inducibly phosphorylated, but this phosphorylation is dispensable for the interaction with CBP/p300. Constitutive active versions of c-Raf and Rac synergistically enhance the CBP/p300-mediated increase of TAD-A activity, indicating the important role CBP/p300 plays in the integration of T cell activation signals. Since a mutation of CBP abolishing HAT activity is almost as active as wild-type CBP in T cells, functions of CBP/p300 other than histone acetylation appear to control the NF-AT-dependent transcription in T cells."}

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