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2. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function.

Author

Torchia J, Rose DW, Inostroza J, Kamei Y, Westin S, Glass CK, and Rosenfeld MG

Subjects
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 antagonists & inhibitors, Interferon-gamma metabolism, Leucine metabolism, Molecular Sequence Data, Nuclear Receptor Coactivator 1, Nuclear Receptor Coactivator 2, Nuclear Receptor Coactivator 3, Protein Binding, Rats, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Signal Transduction, Trans-Activators genetics, Transcription Factors genetics, Transcriptional Activation, Tretinoin antagonists & inhibitors, Tretinoin metabolism, Nuclear Proteins metabolism, Receptors, Cytoplasmic and Nuclear metabolism, Trans-Activators metabolism, Transcription Factors metabolism
Abstract

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.

Published
1997
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