USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-β type I receptor

@article{Zhang2012USP4IR,
  title={USP4 is regulated by AKT phosphorylation and directly deubiquitylates TGF-β type I receptor},
  author={Long Zhang and Fangfang Zhou and Yvette Drabsch and Rui Gao and B. Ewa Snaar-Jagalska and Craig Mickanin and Huizhe Huang and Kelly-Ann Sheppard and Jeff A. Porter and Chris Xiaoxuan Lu and Peter ten Dijke},
  journal={Nature Cell Biology},
  year={2012},
  volume={14},
  pages={717-726}
}
The stability and membrane localization of the transforming growth factor-β (TGF-β) type I receptor (TβRI) determines the levels of TGF-β signalling. TβRI is targeted for ubiquitylation-mediated degradation by the SMAD7–SMURF2 complex. Here we performed a genome-wide gain-of-function screen and identified ubiquitin-specific protease (USP) 4 as a strong inducer of TGF-β signalling. USP4 was found to directly interact with TβRI and act as a deubiquitylating enzyme, thereby controlling TβRI levels… CONTINUE READING
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