title: [Histone demethylase LSD1 and its biological functions].
abstract: Discovery of histone lysine specific demethylase 1 (LSD1) indicates that even histone methylation is reversible. Structural analysis shows that LSD1 is a flavin-dependent amine oxidase, which is able to catalyze the specific removal of methyl groups from mono- and dimethylated Lys4 and Lys9 of histone H3. Functional studies demonstrate that LSD1 regulates activation and inhibition of gene transcription in the nucleus, which is known as the innermost gene switch of cells. LSD1 plays important roles in embryonic development and tumorigenesis. Here, we review recent insights into the structure and chemical mechanism of LSD1, and its regulatory roles in development and cancer.
authors.affiliation: Institute of Basic Medical Science, School of Medicine, Jiangsu University, Zhenjiang 212013, China. gbshao07@ujs.edu.cn
authors.forename: Gen-Bao
authors.initials: GB
authors.lastname: Shao
authors.forename: Xiao-Jia
authors.initials: XJ
authors.lastname: Huang
authors.forename: Ai-Hua
authors.initials: AH
authors.lastname: Gong
authors.forename: Zhi-Jian
authors.initials: ZJ
authors.lastname: Zhang
authors.forename: Rong-Zhu
authors.initials: RZ
authors.lastname: Lu
authors.forename: Jian-Rong
authors.initials: JR
authors.lastname: Sang
mesh_terms: D000818:Animals; D047108:Embryonic Development; D056466:Histone Demethylases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009369:Neoplasms / Q000378:metabolism / Q000473:pathology
chemical_list: D056466:Histone Demethylases