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

  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},
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
Recent Discussions
This paper has been referenced on Twitter 10 times over the past 90 days. VIEW TWEETS
82 Citations
55 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 82 extracted citations


Publications referenced by this paper.
Showing 1-10 of 55 references

a complex web in cancer progression

  • H. Ikushima, Miyazono, K. TGFβ signalling
  • Nat. Rev. Cancer 10, 415–424
  • 2010
Highly Influential
7 Excerpts

an update

  • Pollak, M. The insulin, insulin-like growth factor receptor family in neoplasia
  • Nat. Rev. Cancer 12, 159–169
  • 2012

Similar Papers

Loading similar papers…