The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation
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The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation. / Fajas, Lluis; Egler, Viviane; Reiter, Raphael; Hansen, Jacob; Kristiansen, Karsten; Debril, Marie-Bernard; Miard, Stéphanie; Auwerx, Johan.
In: Developmental Cell, Vol. 3, No. 6, 2002, p. 903-10.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation
AU - Fajas, Lluis
AU - Egler, Viviane
AU - Reiter, Raphael
AU - Hansen, Jacob
AU - Kristiansen, Karsten
AU - Debril, Marie-Bernard
AU - Miard, Stéphanie
AU - Auwerx, Johan
N1 - 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
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 12479814
VL - 3
SP - 903
EP - 910
JO - Developmental Cell
JF - Developmental Cell
SN - 1534-5807
IS - 6
ER -
ID: 19664081