The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis.

@article{Wang2014TheCM,
  title={The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis.},
  author={Zhanfeng Wang and Minghua Zhang and Shan He and Kefeng Lu and Yuhan Chen and Guichun Xing and Yiming Lu and Ping Liu and Yang Li and Shaoxia Wang and Nan Chai and Jiawei Wu and Haiteng Deng and Hong-rui Wang and Yu Cao and Fei Zhao and Y B Cui and Jianhong Wang and Fuchu He and Lingqiang Zhang},
  journal={Nature communications},
  year={2014},
  volume={5},
  pages={3733}
}
Neddylation, the covalent attachment of ubiquitin-like protein Nedd8, of the Cullin-RING E3 ligase family regulates their ubiquitylation activity. However, regulation of HECT ligases by neddylation has not been reported to date. Here we show that the C2-WW-HECT ligase Smurf1 is activated by neddylation. Smurf1 physically interacts with Nedd8 and Ubc12, forms a Nedd8-thioester intermediate, and then catalyses its own neddylation on multiple lysine residues. Intriguingly, this autoneddylation… CONTINUE READING

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