Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.

  title={Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.},
  author={Zihao Wang and Namrata D Udeshi and Chad Slawson and Philip D. Compton and Kaoru Sakabe and Win Den Cheung and Jeffrey Shabanowitz and Donald F. Hunt and Gerald W. Hart},
  journal={Science signaling},
  volume={3 104},
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 and cytoplasmic proteins. Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown. Here, we identify 141 previously unknown O-GlcNAc sites… CONTINUE READING
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