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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Wu, Yifei Delerive, Philippe Chin, William W. Burris, Thomas P. |
| Abstract | Although PGC-1 (peroxisome proliferator-activated receptor-γ coactivator-1) has been previously shown to enhance thyroid hormone receptor (TR)/retinoid X receptor-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 both in a ligand-dependent and ligand-independent manner and that the extent of coactivation is a function of the thyroid hormone response element examined. Our data also show that PGC-1 stimulation of TR activity in terms of Gal4 DNA-binding domain fusion is strictly ligand-dependent. In addition, an E457A AF-2 mutation had 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 demonstrated 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 ligand-binding domain. Taken together, these results support the notion that PGC-1 is a bona fide TR coactivator and that PGC-1 modulates TR activity via a mechanism different from that utilized with peroxisome proliferator activator receptor-γ. |
| Related Links | http://www.jbc.org/content/277/11/8898.abstract |
| Ending Page | 8905 |
| Starting Page | 8898 |
| Page Count | 8 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 11 |
| Volume Number | 277 |
| DOI | 10.1074/jbc.M110761200 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2002-03-15 |
| Access Restriction | Open |
| Subject Keyword | Thyroid hormone (T3) Thyroid hormone receptor (TR) DNA-binding domain (DBD) Ligand-binding domain (LBD) Thyroid hormone response element (TRE) Peroxisome proliferator-activated receptor (PPAR) Glucocorticoid receptor (GR) Glutathione S-transferase (GST) GENES: STRUCTURE AND REGULATION |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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