The serine protease HtrA2 cleaves UCH-L1 and inhibits its hydrolase activity: implication in the UCH-L1-mediated cell death.

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.

authors

Park DW,Nam MK,Rhim H

doi

10.1016/j.bbrc.2011.09.148

subject

Has Abstract

pub_date

2011-11-11 00:00:00

pages

24-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)01776-1

journal_volume

415

pub_type

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