The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function.
The functionally conserved proteins CBP and p300 act in conjunction with other factors to activate transcription of DNA. A new factor, p/CIP, has been discovered that is present in the cell as a complex with CBP and is required for transcriptional activity of nuclear receptors and other CBP/p300-dependent transcription factors. ... The highly related nuclear-receptor co-activator protein NCoA-1 is also specifically required for ligand-dependent activation of genes by nuclear receptors. p/CIP, NCoA-1 and CBP all contain related leucine-rich charged helical interaction motifs that are required for receptor-specific mechanisms of gene activation, and allow the selective inhibition of distinct signal-transduction pathways.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, CREB-Binding Protein, Cell Line, E1A-Associated p300 Protein, Gene Expression Regulation, Genes, Reporter, Hela Cells, Histone Acetyltransferases, Humans, Interferon-gamma, Leucine, Molecular Sequence Data, Nuclear Proteins, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 2, Nuclear Receptor Coactivator 3, Protein Binding, Rats, Receptors, Cytoplasmic and Nuclear, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Signal Transduction, Trans-Activators, Transcription Factors, Transcriptional Activation, Tretinoin
Amino Acid Sequence, Animals, Binding Sites, CREB-Binding Protein, Cell Line, E1A-Associated p300 Protein, Gene Expression Regulation, Genes, Reporter, Hela Cells, Histone Acetyltransferases, Humans, Interferon-gamma, Leucine, Molecular Sequence Data, Nuclear Proteins, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 2, Nuclear Receptor Coactivator 3, Protein Binding, Rats, Receptors, Cytoplasmic and Nuclear, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Signal Transduction, Trans-Activators, Transcription Factors, Transcriptional Activation, Tretinoin
Nature
Date: Jun. 12, 1997
PubMed ID: 9192892
View in: Pubmed Google Scholar
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