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Journal of Molecular Endocrinology (2005) 35, 503-517    DOI: 10.1677/jme.1.01856
© 2005 Society for Endocrinology
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Scaffold attachment factor B1 directly interacts with nuclear receptors in living cells and represses transcriptional activity

M-B Debril1, L Dubuquoy1, J-N Feige2, W Wahli2, B Desvergne2, J Auwerx1 and L Gelman1,2

1 Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS / INSERM / ULP, BP10142, 67404 Illkirch Cedex, France
2 Center for Integrative Genomics, NCCR Frontiers in Genetics, University of Lausanne, 1015 Lausanne, Switzerland

(Requests for offprints should be addressed to J Auwerx; Email: auwerx{at}igbmc.u-strasbg.fr)

Transcriptional activity relies on coregulators that modify the chromatin structure and serve as bridging factors between transcription factors and the basal transcription machinery. Using the DE domain of human peroxisome proliferator-activated receptor gamma (PPAR{gamma}) as bait in a yeast two-hybrid screen of a human adipose tissue library, we isolated the scaffold attachment factor B1 (SAFB1/HET/HAP), which was previously shown to be a corepressor of estrogen receptor {alpha}. We show here that SAFB1 has a very broad tissue expression profile in human and is also expressed all along mouse embryogenesis. SAFB1 interacts in pull-down assays not only with PPAR{gamma} but also with all nuclear receptors tested so far, albeit with different affinities. The association of SAFB1 and PPAR{gamma} in vivo is further demonstrated by fluorescence resonance energy transfer (FRET) experiments in living cells. We finally show that SAFB1 is a rather general corepressor for nuclear receptors. Its change in expression during the early phases of adipocyte and enterocyte differentiation suggests that SAFB1 potentially influences cell proliferation and differentiation decisions.




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