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An adipogenic cofactor bound by the differentiation domain of PPARgamma.

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.

Pubmed ID: 10393183


  • Castillo G
  • Brun RP
  • Rosenfield JK
  • Hauser S
  • Park CW
  • Troy AE
  • Wright ME
  • Spiegelman BM


The EMBO journal

Publication Data

July 1, 1999

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK-09090
  • Agency: NIDDK NIH HHS, Id: R01 5R37DK31405

Mesh Terms

  • Adipocytes
  • Amino Acid Sequence
  • Animals
  • Azo Compounds
  • Base Sequence
  • Cell Differentiation
  • Cell Line
  • Cloning, Molecular
  • Gene Expression Regulation
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Protein Isoforms
  • RNA, Messenger
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Estrogen
  • Recombinant Fusion Proteins
  • Stem Cells
  • Substrate Specificity
  • Transcription Factors
  • Transcription, Genetic
  • Transfection
  • Yeasts