Differential Use of CREB Binding Protein-Coactivator Complexes

Author:

Kurokawa Riki1234,Kalafus Daniel1234,Ogliastro Marie-Hélène1234,Kioussi Chrissa1234,Xu Lan1234,Torchia Joseph1234,Rosenfeld Michael G.1234,Glass Christopher K.1234

Affiliation:

1. R. Kurokawa, M.-H. Ogliastro, C. K. Glass, Divisions of Cellular and Molecular Medicine and Endocrinology and Metabolism, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093–0651, USA.

2. D. Kalafus, Divisions of Cellular and Molecular Medicine and Endocrinology and Metabolism and Biomedical Sciences Graduate Program, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093–0651, USA.

3. C. Kioussi, J. Torchia, M. G. Rosenfeld, Howard Hughes Medical Institute, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093–0651, USA.

4. L. Xu, Biomedical Sciences Graduate Program, and Howard Hughes Medical Institute, Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093–0651, USA.

Abstract

CREB binding protein (CBP) functions as an essential coactivator of transcription factors that are inhibited by the adenovirus early gene product E1A. Transcriptional activation by the signal transducer and activator of transcription–1 (STAT1) protein requires the C/H3 domain in CBP, which is the primary target of E1A inhibition. Here it was found that the C/H3 domain is not required for retinoic acid receptor (RAR) function, nor is it involved in E1A inhibition. Instead, E1A inhibits RAR function by preventing the assembly of CBP–nuclear receptor coactivator complexes, revealing differences in required CBP domains for transcriptional activation by RAR and STAT1.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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