@article{346283d05c1e11df928f000ea68e967b,
title = "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation",
abstract = "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.",
author = "Lluis Fajas and Viviane Egler and Raphael Reiter and Jacob Hansen and Karsten Kristiansen and Marie-Bernard Debril and St{\'e}phanie Miard and Johan Auwerx",
note = "Keywords: 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",
year = "2002",
language = "English",
volume = "3",
pages = "903--10",
journal = "Developmental Cell",
issn = "1534-5807",
publisher = "Cell Press",
number = "6",
}