title: Epigenetic regulation of adipogenesis by histone methylation.
abstract: Histone methylation is implicated in both gene activation and repression, depending on the specific lysine residue that gets methylated. Recent years have witnessed an explosive expansion of the list of remarkably site-specific histone methyltransferases and demethylases, which greatly facilitates the study on the biological functions of histone methylation in gene expression and cell differentiation in mammalian cells. Adipogenesis represents an excellent model system to understand transcriptional and epigenetic regulation of gene expression and cell differentiation. While transcriptional regulation of adipogenesis has been extensively studied, the roles of epigenetic mechanisms in particular histone methylation in regulation of adipogenesis have just begun to be understood. This review will summarize the recent progress on epigenetic regulation of adipogenesis by histone methylation, with a focus on histone H3K4 and H3K27. The available evidence suggests that site-specific histone methylations play critical roles in adipogenesis and control the expression of both positive and negative master regulators of adipogenesis. This article is part of a Special Issue entitled: Chromatin in time and space.
authors.affiliation: Adipocyte Biology and Gene Regulation Section, Laboratory of Endocrinology and Receptor Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Health, Bethesda, MD 20892, USA. kaig@niddk.nih.gov
authors.forename: Kai
authors.initials: K
authors.lastname: Ge
mesh_terms: D050156:Adipogenesis / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D044127:Epigenesis, Genetic; D056466:Histone Demethylases / Q000378:metabolism / Q000502:physiology; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D008969:Molecular Sequence Data; D011496:Protein Methyltransferases / Q000378:metabolism / Q000502:physiology; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones; D056466:Histone Demethylases; D011496:Protein Methyltransferases