title: The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation.
abstract: Sir2, an NAD+-dependent protein deacetylase, extends the lifespan in diverse species from yeast to flies. Mammals have seven homologs of Sir2, SIRT1-7, which affect aging and metabolism and which are potential targets for pharmacologic intervention. We identified SIRT2, which preferentially deacetylates tubulin and histone H4, as a downregulated protein in gliomas due to its epigenetic aberration. We herein discuss the role of SIRT2 in the mitotic checkpoint function and show that it may be as a potential target of anti-cancer drugs.
authors: Division of Human Genome Science, Department of Molecular and Cellular Biology, School of Life Sciences, Faculty of Medicine, Tottori University, Yonago, Tottori, Japan. sour@grape.med.tottori-u.ac.jp
authors: Toshiaki
authors: T
authors: Inoue
authors: Masaharu
authors: M
authors: Hiratsuka
authors: Mitsuhiko
authors: M
authors: Osaki
authors: Mitsuo
authors: M
authors: Oshimura
mesh_terms: D000782:Aneuploidy; D000818:Animals; D002453:Cell Cycle / Q000502:physiology*; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D051379:Mice; D008938:Mitosis; D008954:Models, Biological; D009369:Neoplasms / Q000188:drug therapy / Q000378:metabolism; D011123:Polyploidy; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D056565:Sirtuin 2; D037761:Sirtuins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D014404:Tubulin / Q000378:metabolism
chemical_list: D006657:Histones; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae; D014404:Tubulin; C087778:SIR2 protein, S cerevisiae; D056565:Sirtuin 2; D037761:Sirtuins; D006655:Histone Deacetylases