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PLK1 O-GlcNAcylation is essential for dividing mammalian cells and inhibits uterine carcinoma

ABSTRACT: The O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) mediates intracellular O-GlcNAcylation modification, whose function and substrates have entranced biologists and chemists alike. O-GlcNAcylation occurs on Ser/Thr residues and takes part in a vast array of physiological processes. OGT is essential for dividing mammalian cells, and it underscores many human diseases. Yet many of its fundamental substrates in the cell division process remains to be unveiled. Here we focus on its effect on Polo-like kinase 1 (PLK1), a mitotic master kinase that governs DNA replication, mitotic entry, chromosome segregation and mitotic exit. We found that PLK1 interacts with OGT and is O-GlcNAcylated.

ORGANISM(S): Homo Sapiens

SUBMITTER: Jing Li

PROVIDER: PXD036141 | iProX | Wed Aug 17 00:00:00 BST 2022

REPOSITORIES: iProX

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Polo-like kinase 1 (PLK1) O-GlcNAcylation is essential for dividing mammalian cells and inhibits uterine carcinoma.

Yan Sheng S Peng Bin B Kan Shifeng S Shao Guangcan G Xiahou Zhikai Z Tang Xiangyan X Chen Yong-Xiang YX Dong Meng-Qiu MQ Liu Xiao X Xu Xingzhi X Li Jing J

The Journal of biological chemistry 20230107 2

The O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) mediates intracellular O-GlcNAcylation modification. O-GlcNAcylation occurs on Ser/Thr residues and is important for numerous physiological processes. OGT is essential for dividing mammalian cells and is involved in many human diseases; however, many of its fundamental substrates during cell division remain unknown. Here, we focus on the effect of OGT on polo-like kinase 1 (PLK1), a mitotic master kinase that governs DNA replication ...[more]

PMID: 36626982

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