| Literature DB >> 27080259 |
Jie Tian1, Qizhi Geng1, Yuehe Ding2, Ji Liao1, Meng-Qiu Dong2, Xingzhi Xu3, Jing Li4.
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.Entities:
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
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Year: 2016 PMID: 27080259 PMCID: PMC4933264 DOI: 10.1074/jbc.M116.717850
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157