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Nature 387, 677-684 (12 June 1997) | ; Received 14 January 1997; Accepted 6 May 1997

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

Joseph Torchia1, David W. Rose2, Juan Inostroza1, Yasutomi Kamei1, Stefan Westin3, Christopher K. Glass3 & Michael G. Rosenfeld1

  1. Howard Hughes Medical Institute, University of California,San Diego, 9500 Gilman Drive, La Jolla, California 92093-0648, USA
  2. UCSD Department of Medicine and Whittier Diabetes Program, University of California,San Diego, 9500 Gilman Drive, La Jolla, California 92093-0648, USA
  3. Cellular and Molecular Medicine, School and Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0648, USA

Correspondence to: David W. Rose2Michael G. Rosenfeld1 Correspondence should be addressed to D.W.R. and requests for materials to M.G.R.

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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.