Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.

@article{Kapuria2016ProteolysisOH,
  title={Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.},
  author={Vaibhav Kapuria and Ute F. R{\"o}hrig and Tanja Bhuiyan and Vladimir S Borodkin and Daan M F van Aalten and Vincent Zoete and Winship Herr},
  journal={Genes & development},
  year={2016},
  volume={30 8},
  pages={
          960-72
        }
}
In complex with the cosubstrate UDP-N-acetylglucosamine (UDP-GlcNAc),O-linked-GlcNAc transferase (OGT) catalyzes Ser/ThrO-GlcNAcylation of many cellular proteins and proteolysis of the transcriptional coregulator HCF-1. Such a dual glycosyltransferase-protease activity, which occurs in the same active site, is unprecedented and integrates both reversible and irreversible forms of protein post-translational modification within one enzyme. Although occurring within the same active site, we show… CONTINUE READING
2
Twitter Mentions

References

Publications referenced by this paper.
SHOWING 1-10 OF 35 REFERENCES

HCF - 1 iscleavedinthe active site of O - GlcNAc transferase

MB Lazarus, J Jiang, +4 authors WalkerS HerrW
  • Science
  • 2013
VIEW 23 EXCERPTS
HIGHLY INFLUENTIAL

Proteolytic Cleavage Driven by Glycosylation.

  • The Journal of biological chemistry
  • 2016
VIEW 3 EXCERPTS
HIGHLY INFLUENTIAL

Similar Papers

Loading similar papers…