This work was supported by grants from The National Natural Science Foundation of China(90408011), The National Basic Research Program of China (2006CB102103), and the Program for New Century Excellent Talents in University and the Key Project of Chinese Ministry of Education(NCET-05-0620).
UCH-L1 (ubiquitin carboxy-terminal hydrolases L1) is a member of the carboxyl-terminal ubiquitin hydrolase family, naturally, that there is hydrolase activity, however, and that there is ligase acitivity, which is different from the other members of UCHs. UCH-L1 hydrolase activity could keep the pool of free ubiquitin and compromise the ubiquitin-dependent degradation pathway, while UCH-L1 dimerizational-dependent, ubiquityl ligase activity could produce undegradable, K63-linked polyubiquitin chains that could inhibit proteasomal activity. Therefore, UCH-L1 is involved in the more diverse physiological activities, including neuron formation, gonadal development and fertilization. Mutation of UCH-L1 is linked to the neurodegenerative diseases, such as Parkinson's disease. Moreover, abnormal expression of UCH-L1 is response to carcinogenesis in many tissue such as thyroid lung.
SUN Jin-Hua, CHENG Han-Hua, ZHOU Rong-Jia. Ubiquitin C-terminal Hydrolases L1:Physiological and Pathological Significance[J]. Progress in Biochemistry and Biophysics,2007,34(8):800-805
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