USP7 (Ubiquitin-Specific Protease 7)
Proteins are vital to the structure and functioning of cells, and so the regulated turnover of proteins is an absolute essential of cellular metabolism. This necessity for the major part has been found to be taken care of by the ubiquitin-proteasome system (UPS). The system was discovered as a result of the work carried out by Avram Hershko, Aaron Ciechanover, and Irwin Rose, for which they shared the 2004 Nobel Prize in Chemistry. The UPS in its most simplified form consists of a tagging factor in the form of the small protein ubiquitin, enzymes that mediate the tagging of unwanted or damaged proteins, and the proteasome, a large molecular shredder that cleaves tagged proteins in to smaller peptides for use in other anabolic processes. More than 80% of all cellular proteins undergo degradation by the UPS, highlighting its importance in regulating various eukaryotic cellular processes such as cell cycle progression, stress response,...
Financially supported by grants from CSIR, India (EMPOWER-OLP-002, MEDCHEM-BSC0108 & CSIR-MAYO: MLP-0017), and DST Nano Mission program (SR/NM/NS-1058/2015) to Dr. Mrinal K Ghosh.
Conflict of Interest The authors declare no conflict of interest.
- Bhattacharya S, Ghosh MK. Cell death and deubiquitinases: perspectives in cancer. BioMed Res Int. 2014a. Article ID 435197.Google Scholar
- Hu M, Li P, Li M, Li W, Yao T, Wu J-W, Gu W, Cohen RE, Shi Y. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell. 2002;111:1041–54.Google Scholar