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A more recent version of this article appeared on February 10, 2006
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M510403200v1
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Papers In Press, published online ahead of print December 12, 2005
J. Biol. Chem, 10.1074/jbc.M510403200
Submitted on September 22, 2005
Accepted on December 12, 2005

Differential use of functional domains by CoCoA in its synergistic coactivator function with beta -catenin or GRIP1

Catherine K. Yang, Jeong Hoon Kim, Hongwei Li, and Michael R. Stallcup

Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90089-9151

Corresponding Author: stallcup{at}usc.edu

beta -catenin, a pivotal component of the Wnt-signaling pathway, binds to and serves as a transcriptional coactivator for the T-Cell Factor/Lymphoid Enhancer Factor (TCF/LEF) family of transcriptional activator proteins, and also for the androgen receptor (AR), a nuclear receptor. Three components of the p160 nuclear receptor coactivator complex, including CARM1, p300/CBP, and GRIP1 (one of the p160 coactivators), bind to and cooperate with beta -catenin to enhance transcriptional activation by TCF/LEF and AR. Here we report that another component of the p160 nuclear receptor coactivator complex, the coiled-coil coactivator (CoCoA), directly binds to and cooperates synergistically with beta -catenin as a coactivator for AR and TCF/LEF. CoCoA uses different domains to bind GRIP1 and beta -catenin, and it uses different domains to transmit the activating signal to the transcription machinery, depending on whether it is bound to GRIP1 or beta -catenin. CoCoA associated specifically with the promoters of transiently transfected and endogenous target genes of TCF/LEF, and reduction of the endogenous CoCoA level decreased the ability of TCF/LEF and beta -catenin to activate transcription of transient and endogenous target genes. Thus, CoCoA uses different combinations of functional domains to serve as a physiologically relevant component of the Wnt/beta -catenin signaling pathway and the androgen signaling pathway.


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