SUMOylation and PPARgamma: wrestling with inflammatory signaling.
The molecular mechanisms whereby PPARgamma inhibits inflammatory gene expression in macrophages are poorly understood. In a recent Nature paper, provide a new model for trans-repression in which ligand-dependent SUMOylation of PPARgamma results in its recruitment to the promoters of inflammatory genes where it inhibits transcription by preventing clearance of corepressor complexes.
Zelcer
Noam
N
Howard Hughes Medical Institute, Department of Pathology and Laboratory Medicine, University of California, Los Angeles, Los Angeles, California 90055, USA.
Tontonoz
Peter
P
D000818:Animals; D007249:Inflammation / Q000235:genetics* / Q000378:metabolism; D008070:Lipopolysaccharides; D008264:Macrophages / Q000187:drug effects / Q000378:metabolism; D051379:Mice; D046912:Multiprotein Complexes / Q000378:metabolism; D052247:Nitric Oxide Synthase Type II / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000096:biosynthesis / Q000378:metabolism*; D056971:Nuclear Receptor Co-Repressor 1; D047495:PPAR gamma / Q000819:agonists / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D012097:Repressor Proteins / Q000096:biosynthesis / Q000378:metabolism*; D025842:SUMO-1 Protein / Q000378:metabolism*
D008070:Lipopolysaccharides; D046912:Multiprotein Complexes; C539128:Ncor1 protein, mouse; D009687:Nuclear Proteins; D056971:Nuclear Receptor Co-Repressor 1; D047495:PPAR gamma; D012097:Repressor Proteins; D025842:SUMO-1 Protein; D052247:Nitric Oxide Synthase Type II