Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.

@article{Wang2010ExtensiveCB,
  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},
  year={2010},
  volume={3 104},
  pages={ra2}
}
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
Related Discussions
This paper has been referenced on Twitter 2 times. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 120 extracted citations

O-GlcNAc: A Sweetheart of the Cell Cycle and DNA Damage Response

Front. Endocrinol. • 2018
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…