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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2002-12-13
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidinediones,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/histone deacetylase 3,
http://linkedlifedata.com/resource/pubmed/chemical/rosiglitazone
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1534-5807
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
903-10
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12479814-3T3 Cells,
pubmed-meshheading:12479814-Adipocytes,
pubmed-meshheading:12479814-Animals,
pubmed-meshheading:12479814-Cell Differentiation,
pubmed-meshheading:12479814-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:12479814-Genes, Reporter,
pubmed-meshheading:12479814-Histone Deacetylases,
pubmed-meshheading:12479814-Lipoprotein Lipase,
pubmed-meshheading:12479814-Macromolecular Substances,
pubmed-meshheading:12479814-Mice,
pubmed-meshheading:12479814-Phosphorylation,
pubmed-meshheading:12479814-Protein Binding,
pubmed-meshheading:12479814-Protein Structure, Tertiary,
pubmed-meshheading:12479814-RNA, Messenger,
pubmed-meshheading:12479814-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:12479814-Recombinant Fusion Proteins,
pubmed-meshheading:12479814-Retinoblastoma Protein,
pubmed-meshheading:12479814-Signal Transduction,
pubmed-meshheading:12479814-Stem Cells,
pubmed-meshheading:12479814-Thiazoles,
pubmed-meshheading:12479814-Thiazolidinediones,
pubmed-meshheading:12479814-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation.
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pubmed:affiliation |
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 67404 Illkirch, France.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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