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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

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.[1]

References

  1. The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation. Fajas, L., Egler, V., Reiter, R., Hansen, J., Kristiansen, K., Debril, M.B., Miard, S., Auwerx, J. Dev. Cell (2002) [Pubmed]
 
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