title: O-GlcNAcylation Antagonizes Phosphorylation of CDH1 (CDC20 Homologue 1).
abstract: The anaphase promoting complex/cyclosome (APC/C) orchestrates various aspects of the eukaryotic cell cycle. One of its co-activators, Cdh1, is subject to myriad post-translational modifications, such as phosphorylation and ubiquitination. Herein we identify the O-linked N-acetylglucosamine (O-GlcNAc) modification that occurs on Cdh1. Cdh1 is O-GlcNAcylated in cultured cells and mouse brain extracts. Mass spectrometry identifies an O-GlcNAcylated peptide that neighbors a known phosphorylation site. Cell synchronization and mutation studies reveal that O-GlcNAcylation of Cdh1 may antagonize its phosphorylation. Our results thus reveal a pivotal role of O-GlcNAcylation in regulating APC/C activity.
authors.affiliation: From the Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing 100048, China and.
authors.forename: Jie
authors.initials: J
authors.lastname: Tian
authors.affiliation: From the Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing 100048, China and.
authors.forename: Qizhi
authors.initials: Q
authors.lastname: Geng
authors.affiliation: National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Yuehe
authors.initials: Y
authors.lastname: Ding
authors.affiliation: From the Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing 100048, China and.
authors.forename: Ji
authors.initials: J
authors.lastname: Liao
authors.affiliation: National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Meng-Qiu
authors.initials: MQ
authors.lastname: Dong
authors.affiliation: From the Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing 100048, China and xingzhi_xu@cnu.edu.cn.
authors.forename: Xingzhi
authors.initials: X
authors.lastname: Xu
authors.affiliation: From the Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing 100048, China and jing_li@cnu.edu.cn.
authors.forename: Jing
authors.identifier: 0000-0002-3977-1641
authors.initials: J
authors.lastname: Li
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000215:Acylation; D064173:Anaphase-Promoting Complex-Cyclosome / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D064200:Cdh1 Proteins / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006367:HeLa Cells; D006801:Humans; D015151:Immunoblotting; D051379:Mice; D009154:Mutation; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D053719:Tandem Mass Spectrometry
chemical_list: D064200:Cdh1 Proteins; D064173:Anaphase-Promoting Complex-Cyclosome; D017351:N-Acetylglucosaminyltransferases; D000117:Acetylglucosamine
keywords: Cdh1; O-linked N-acetylglucosamine (O-GlcNAc); O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT); anaphase promoting complex/cyclosome (APC/C); cell cycle; mitosis; phosphorylation