| First Author | Castillo G | Year | 1999 |
| Journal | EMBO J | Volume | 18 |
| Issue | 13 | Pages | 3676-87 |
| PubMed ID | 10393183 | Mgi Jnum | J:56274 |
| Mgi Id | MGI:1340727 | Doi | 10.1093/emboj/18.13.3676 |
| Citation | Castillo G, et al. (1999) An adipogenic cofactor bound by the differentiation domain of PPARgamma. EMBO J 18(13):3676-87 |
| abstractText | Ligand activation of the nuclear receptor PPARgamma induces adipogenesis and increases insulin sensitivity, while activation of other PPAR isoforms (-alpha and -delta) induces little or no fat cell differentiation. Expression and activation of chimeras formed between PPARgamma and PPARdelta in fibroblasts has allowed us to localize a major domain of PPARgamma responsible for adipogenesis to the N-terminal 138 amino acids, a region with AF-1 transcriptional activity. Using this region of PPARgamma as bait, we have used a yeast two-hybrid screen to clone a novel protein, termed PGC-2, containing a partial SCAN domain. PGC-2 binds to and increases the transcriptional activity of PPARgamma but does not interact with other PPARs or most other nuclear receptors. Ectopic expression of PGC-2 in preadipocytes containing endogenous PPARgamma causes a dramatic increase in fat cell differentiation at both the morphological and molecular levels. These results suggest that interactions between PGC-2, a receptor isoform-selective cofactor and PPARgamma contribute to the adipogenic action of this receptor. |
