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A more recent version of this article appeared on March 8, 2002
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M110761200v1
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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

Requirement of helix 1 and the AF-2 domain of thyroid hormone receptor for coactivation by PGC-1

Yifei Wu, Philippe Delerive, William W. Chin, and Thomas P. Burris

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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