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Papers In Press, published online ahead of print December 20, 2001
J. Biol. Chem, 10.1074/jbc.M110761200
Submitted on November 9, 2001
Revised on December 19, 2001
Accepted on December 20, 2001
Department of Gene Regulation, Bone and Inflammation Research, Eli Lilly and Company, Indianapolis, IN 46285
Corresponding Author: burris_thomas_p{at}lilly.com
Although PPAR gamma coactivator 1 (PGC-1) has been previously shown to enhance TR/RXR mediated ucp-1 gene expression in a ligand-induced manner in rat fibroblast cells, the precise mechanism of PGC-1 modulation of TR function has yet to be determined. In this study, we show that PGC-1 can potentiate TR-mediated transactivation of reporter genes driven by natural thyroid hormone response elements (TREs) both in a ligand-dependent and ligand-independent manner and the extent of coactivation is a function of the TRE examined. Our data also show that PGC-1 stimulation of TR activity in the terms of Gal4-DNA binding domain fusion is strictly ligand-dependent when examined. In addition, an E457A AF-2 mutation has no effect on the ligand-induced PGC-1 enhancement of TR activity, indicating that the conserved charged residue in AF-2 is not essential for this PGC-1 function. Furthermore, GST pull-down and mammalian two hybrid assays demonstrate that the PGC-1 LXXLL motif is required for ligand-induced PGC-1-TR interaction. This agonist-dependent PGC-1-TR interaction also requires both helix 1 and the AF-2 region of the TR LBD. Taken together, these results support the notion that PGC-1 is a bona fide TR coactivator and PGC-1 modulates TR activity via a mechanism different from that utilized with PPAR gamma.
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