作者:
Jingdong Cheng (1) (2)Ze Li (1) (2)Rui Gong (1)Jian Fang (1)Yi Yang (1)Chang Sun (1)Huirong Yang (1)Yanhui Xu (1) (2) (3)1.keylaboratory of Molecular Medicine
Ministry of Education Department of Systems Biology for Medicine School of Basic Medical Sciences Shanghai Medical College of Fudan University Shanghai 200032 China 2.School of Basic Medical Sciences Fudan University Shanghai Cancer Center Institutes of Biomedical Sciences Shanghai Medical College of Fudan University Shanghai 200032 China 3.State Key Laboratory of Genetic Engineering School of Life Sciences Collaborative Innovation Center of Genetics and Development Fudan University Shanghai 200433 China
Dear Editor, The ubiquitin specific protease 7 (USP7), also known as herpes virus associated ubiquitin specific protease (HAUSP), is a well-characterized deubiquitinase (Reyes- Turcu et al., 2009). USP7 plays im...
详细信息
Dear Editor, The ubiquitin specific protease 7 (USP7), also known as herpes virus associated ubiquitin specific protease (HAUSP), is a well-characterized deubiquitinase (Reyes- Turcu et al., 2009). USP7 plays important roles in various biological processes, including cell survival, proliferation, apoptosis, tumorigenesis, viral infection, and epigenetic regulation through regulating the protein stability of tumor suppressors (p53, PTEN, FOXO, claspin), E3 ligases (MDM2, Mule, viral proteins ICP0), epigenetic regulators (DNMT1, Tip60, UHRF1) (Pfoh et al., 2015). USP7 is comprised of three recognizable domains: the N-terminal TRAF domain, the catalytic domain, and the C-terminal Tandem UBL domain (designated TUDusPT) (Fig. 1A). Previous study shows that the TRAF domain binds to P/AxxS motif (from p53 and MDM2) and is responsible for substrate recognition (Sheng et al., 2006). However, how USP7 recognizes other substrates remains largely unknown.
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