Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors.

Transcriptional coactivators either bridge transcription factors and the components of the basal transcription apparatus and/or remodel the chromatin structures. We isolated a novel nuclear protein based on its interaction with the recently described general coactivator activating signal cointegrator-2 (ASC-2). This protein CAPER (for coactivator of activating protein-1 (AP-1) and estrogen ...
receptors (ERs)) selectively bound, among the many transcription factors we tested, the AP-1 component c-Jun and the estradiol-bound ligand binding domains of ERalpha and ERbeta. Interestingly, CAPER exhibited a cryptic autonomous transactivation function that becomes activated only in the presence of estradiol-bound ER. In cotransfections, CAPER stimulated transactivation by ERalpha, ERbeta, and AP-1. Thus, CAPER may represent a more selective transcriptional coactivator molecule that plays a pivotal role for the function of AP-1 and ERs in vivo in conjunction with the general coactivator ASC-2.
Mesh Terms:
Amino Acid Motifs, Animals, Cell Line, Cloning, Molecular, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Nuclear Proteins, Nuclear Receptor Coactivators, Protein Binding, Proto-Oncogene Proteins c-jun, RNA-Binding Proteins, Receptors, Estrogen, Recombinant Fusion Proteins, Sequence Alignment, Trans-Activators, Transcription Factor AP-1, Transcription Factors, Transcriptional Activation, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Jan. 11, 2002
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