Extensive Crosstalk Between O-GlcNAcylation and Phosphorylation Regulates Cytokinesis

• DOI: 10.1126/scisignal.2000526
• Publication Date: 2010-01-12T23:52:56Z
• Authors: Zihao Wang; Namrata D. Udeshi; Chad Slawson; Philip D. Compton; Kaoru Sakabe; Win D. Cheung; Jeffrey Shabanowitz; Donald F. Hunt; Gerald W. Hart
• Keywords: Midbody; Crosstalk

Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear cytoplasmic proteins. Overexpression enzyme adds O-GlcNAc to target proteins, transferase (OGT), perturbs cytokinesis promotes polyploidy, but molecular targets OGT are important for its cell cycle functions unknown. Here, we identify 141 previously unknown sites proteins function in spindle assembly cytokinesis. Many these O-GlcNAcylation either identical known phosphorylation or close proximity them. Furthermore, found altered key associated with mitotic midbody. Forced overexpression increased inhibitory cyclin-dependent kinase 1 (CDK1) reduced CDK1 The explained by activation upstream kinase, MYT1, concomitant reduction transcript phosphatase, CDC25C. also caused both messenger RNA expression protein abundance Polo-like 1, which MYT1 data not only illustrate crosstalk between regulators crucial signaling pathways uncover mechanism role regulation division.