The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier

@article{Wang2011TheDR,
  title={The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier},
  author={Fengbin Wang and Meiruo Liu and Rui Qiu and Chaoneng Ji},
  journal={Protein & Cell},
  year={2011},
  volume={2},
  pages={612-619}
}
The ubiquitin-related modifier Urm1 can be covalently conjugated to lysine residues of other proteins, such as yeast Ahp1 and human MOCS3, through a mechanism involving the E1-like protein Uba4 (MOCS3 in humans). Similar to ubiquitination, urmylation requires a thioester intermediate and forms isopeptide bonds between Urm1 and its substrates. In addition, the urmylation process can be significantly enhanced by oxidative stress. Recent findings have demonstrated that Urm1 also acts as a sulfur… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 59 references

Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier

A. G. Van der Veen, K. Schorpp, +5 authors S. Jentsch
Proc Natl Acad Sci U S A • 2011
View 12 Excerpts
Highly Influenced

Evolution and function of ubiquitin-like protein-conjugation systems

Nature Cell Biology • 2000
View 8 Excerpts
Highly Influenced

Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress.

Proceedings of the National Academy of Sciences of the United States of America • 2011
View 4 Excerpts
Highly Influenced

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