PubMed:10358178 JSONTXT

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"S2","span":{"begin":102,"end":250},"obj":"Sentence"},{"id":"S3","span":{"begin":251,"end":434},"obj":"Sentence"},{"id":"S4","span":{"begin":435,"end":618},"obj":"Sentence"},{"id":"S5","span":{"begin":619,"end":837},"obj":"Sentence"},{"id":"S6","span":{"begin":838,"end":1061},"obj":"Sentence"},{"id":"S7","span":{"begin":1062,"end":1157},"obj":"Sentence"},{"id":"S8","span":{"begin":1158,"end":1315},"obj":"Sentence"}],"text":"Multiple NF-ATc isoforms with individual transcriptional properties are synthesized in T lymphocytes.\nThe transcription factor NF-ATc that controls gene expression in T lymphocytes and embryonic cardiac cells is expressed in three prominent isoforms. This is due to alternative splice/polyadenylation events that lead to the predominant synthesis of two long isoforms in naive T cells and a shorter NF-ATc isoform in effector T cells. Whereas the previously described isoform NF-ATc/A contains a relatively short C terminus, the longer isoforms, B and C, span extra C-terminal peptides of 128 and 246 aa, respectively. We show here that in addition to the strong N-terminal trans-activation domain, TAD-A, which is common to all three NF-ATc isoforms, NF-ATc/C contains a second trans-activation domain, TAD-B, in its C-terminal peptide. Various stimuli of T cells that induce the activity of TAD-A also enhance the activity of TAD-B, but, unlike TAD-A, TAD-B remains unphosphorylated by protein from 12-O-tetradecanoyl 12-phorbol 13-acetate-stimulated T cells. The shorter C-terminal peptide of isoform NF-ATc/B exerts a suppressive transcriptional effect. These properties of NF-ATc/B and -C might be of importance for gene regulation in naive T lymphocytes in which NF-ATc/B and -C are predominantly synthesized."}

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