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pubmed-article:7870179pubmed:dateCreated1995-3-30lld:pubmed
pubmed-article:7870179pubmed:abstractTextThe 265K nuclear protein CBP was initially identified as a co-activator for the protein kinase A (PKA)-phosphorylated form of the transcription factor CREB. The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral E1A-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown. Here, we show that CBP and p300 have similar binding affinity for the PKA-phosphorylated form of CREB, and that p300 can substitute for CBP in potentiating CREB-activated gene expression. We find that E1A binds to CBP through a domain conserved with p300 and represses the CREB-dependent co-activator functions of both CBP and p300. Our results indicate that the gene repression and cell immortalization functions associated with E1A involve the inactivation of a family of related proteins that normally participate in second-messenger-regulated gene expression.lld:pubmed
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pubmed-article:7870179pubmed:pagination85-8lld:pubmed
pubmed-article:7870179pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:7870179pubmed:year1995lld:pubmed
pubmed-article:7870179pubmed:articleTitleAdenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP.lld:pubmed
pubmed-article:7870179pubmed:affiliationVollum Institute, Oregon Health Sciences University, Portland 97201.lld:pubmed
pubmed-article:7870179pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7870179pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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