Abstract:
:Ubiquitin (Ub) carboxyl-terminal hydrolase L1 (UCH-L1) has dual functions, such as hydrolase activity on the chemical bonds formed by the C-terminal Gly of Ub and dimerization-dependent ubiquitin ligase activity. Accumulating evidence suggests that dual activities of UCH-L1 were intimately associated with Parkinson's diseases (PD) and cancer. However, the molecular mechanism that regulates UCH-L1 enzymatic activity has not yet been fully elucidated. The serine protease high temperature requirement A2 (HtrA2), a PD-associated gene, is important in regulating cell survival as well as apoptosis. Using in vitro and in vivo cleavage assays, we have demonstrated that UCH-L1 is a natural substrate for the serine protease HtrA2 in the apoptotic pathway. Notably, we show that released, cytosolic HtrA2 decreases UCH-L1 protein level and its hydrolase activity through HtrA2-mediated cleavage of UCH-L1 under apoptotic conditions. These findings suggest that the HtrA2-mediated cleavage of UCH-L1 may play important roles in regulating the fine balance between cell growth and cell death.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Park DW,Nam MK,Rhim Hdoi
10.1016/j.bbrc.2011.09.148subject
Has Abstractpub_date
2011-11-11 00:00:00pages
24-9issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(11)01776-1journal_volume
415pub_type
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