Article

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

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 and 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.

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.

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