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Ubiquitin carboxy-terminal hydrolase L1 is a deubiquitinating enzyme. Enzymes from this thiol-protease family hydrolyse ubiquitin from the C-terminal end of substrates to generate the ubiquitin monomers, the active component of the cell’s ubiquitin dependent proteolytic system, which degrades damaged proteins. A second function of UCHL1 has since been described: as a dimer, UCHL1 ubiquitinylates selective substrates in an ATPase-independent reaction.
UCHL1 is expressed predominantly in neurons and in cells of the diffuse neuroendocrine system and their tumors. Mutations in this gene are implicated as the cause of Parkinson’s and Alzheimer’s diseases. Improper function of this enzyme affects protein degradation pathways leading to misfolded proteins accumulation such as alpha-synuclein and consequently to neurodegeneration pathology (see molecular model below).

Fluorescent image of U251 cell stained with UCHL1 Antibody (C-term) (Cat#AP2126e/SA120806AG). U251 cells were fixed with 4% PFA (20 min), permeabilized with Triton X-100 (0.1%, 10 min), then incubated with UCHL1 primary antibody (1:25, 1 h at 37°C). For secondary antibody, Alexa Fluor® 488 conjugated donkey anti-rabbit antibody (green) was used (1:400, 50 min at 37°C). Cytoplasmic actin was counterstained with Alexa Fluor® 555 (red) conjugated Phalloidin (7units/ml, 1 h at 37°C). UCHL1 is localized to cytoplasm and nucleus.

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UCHL1 ()