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Papers In Press, published online ahead of print September 28, 2000
J. Biol. Chem, 10.1074/jbc.M005459200
Submitted on June 22, 2000
Accepted on September 27, 2000

Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300

Dagang Chen, Shih-Ming Huang, and Michael R. Stallcup

Pathology, University of Southern California, Los Angeles, CA 90089

Corresponding Author: stallcup{at}usc.edu

Members of the p160 coactivator family (SRC-1, GRIP1, and ACTR) mediate transcriptional activation by nuclear receptors (NR). After being recruited to the promoter by NR, the p160 coactivator transmits the activating signal via two C-terminal activation domains, AD1 and AD2. AD1 is a binding site for the related coactivators CBP and p300, while AD2 binds to another coactivator CARM1, a protein arginine methyltransferase. The current study explored the cooperative functional and mechanistic relationships among GRIP1, CARM1, and p300 in transient transfection assays, where they enhanced the ability of the estrogen receptor (ER) to activate transcription of a reporter gene. The coactivator functions of p300 and CARM1 depended on the co-expression of GRIP1. Simultaneous co-expression of all three coactivators caused a synergistic enhancement of ER function. Deletion of the AD1 domain of GRIP1 abolished the ability of p300 to potentiate the ER transcription but had no effect on the CARM1-mediated transcriptional stimulation. In contrast, when the AD2 domain of GRIP1 was deleted, p300 still stimulated ER function through the mutant GRIP1, but CARM1 failed to do so. Thus, both binding of p300 to AD1 and binding of CARM1 to AD2 are required for their respective coactivator functions and for their synergy. Furthermore, CARM1 and p300 function independently through different activating domains of GRIP1, and their synergy suggests that they enhance transcription by different, complementary mechanisms.


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