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  • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility.

The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility.

Cell (2002-11-01)
Yichin Liu, Lara Fallon, Hilal A Lashuel, Zhihua Liu, Peter T Lansbury
ABSTRACT

The assumption that each enzyme expresses a single enzymatic activity in vivo is challenged by the linkage of the neuronal enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) to Parkinson's disease (PD). UCH-L1, especially those variants linked to higher susceptibility to PD, causes the accumulation of alpha-synuclein in cultured cells, an effect that cannot be explained by its recognized hydrolase activity. UCH-L1 is shown here to exhibit a second, dimerization-dependent, ubiquityl ligase activity. A polymorphic variant of UCH-L1 that is associated with decreased PD risk (S18Y) has reduced ligase activity but comparable hydrolase activity as the wild-type enzyme. Thus, the ligase activity as well as the hydrolase activity of UCH-L1 may play a role in proteasomal protein degradation, a critical process for neuronal health.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Ubiquitin C-terminal hydrolase L1 (UCH-L1), 50 µg, From human cDNA, expressed in E. coli. Ubiquitin C-terminal hydrolases are a family of cysteine hydrolases that catalyze the hydrolysis of amides, esters & thioesters of the C-terminus of ubiquitin.
Sigma-Aldrich
UCHL1, His tagged human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution