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The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation.

Developmental cell | Dec 13, 2002

http://www.ncbi.nlm.nih.gov/pubmed/12479814

The retinoblastoma protein (RB) has previously been shown to facilitate adipocyte differentiation by inducing cell cycle arrest and enhancing the transactivation by the adipogenic CCAAT/enhancer binding proteins (C/EBP). We show here that the peroxisome proliferator-activated receptor gamma (PPARgamma), a nuclear receptor pivotal for adipogenesis, promotes adipocyte differentiation more efficiently in the absence of RB. PPARgamma and RB were shown to coimmunoprecipitate, and this PPARgamma-RB complex also contains the histone deacetylase HDAC3, thereby attenuating PPARgamma's capacity to drive gene expression and adipocyte differentiation. Dissociation of the PPARgamma-RB-HDAC3 complex by RB phosphorylation or by inhibition of HDAC activity stimulates adipocyte differentiation. These observations underscore an important function of both RB and HDAC3 in fine-tuning PPARgamma activity and adipocyte differentiation.

Pubmed ID: 12479814 RIS Download

Mesh terms: 3T3 Cells | Adipocytes | Animals | Cell Differentiation | Gene Expression Regulation, Enzymologic | Genes, Reporter | Histone Deacetylases | Lipoprotein Lipase | Macromolecular Substances | Mice | Phosphorylation | Protein Binding | Protein Structure, Tertiary | RNA, Messenger | Receptors, Cytoplasmic and Nuclear | Recombinant Fusion Proteins | Retinoblastoma Protein | Signal Transduction | Stem Cells | Thiazoles | Thiazolidinediones | Transcription Factors

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Associated grants

  • Agency: NIDDK NIH HHS, Id: 1 P01-DK59820-01

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