IndraLab

Statements

PRKN inhibits UCHL1. 7 / 7
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"It is reported that interaction with parkin promotes UCHL1 lysosomal degradation [XREF_BIBR] and consequently the lack of parkin could lead to the abnormal UCHL1 accumulation in PD patient cells."
29138676
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"We found that endogenous UCH-L1 protein is a long lived protein with a half-life of ~ 59 hr and the UCH-L1 protein half-life was reduced to ~ 40 hr by parkin overexpression, indicating that parkin indeed promotes UCH-L1 degradation."
25403879
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"We found that parkin overexpression reduced the steady-state level of endogenous UCH-L1 protein (XREF_FIG), consistent with a role of parkin in promoting UCH-L1 degradation."
25403879
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"We find that parkin mediates K63 linked polyubiquitination of UCH-L1 in cooperation with the Ubc13 and Uev1a E2 ubiquitinconjugating enzyme complex and promotes UCH-L1 degradation by the autophagy-lysosome pathway."
25403879
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"Taken together, these results suggest that loss of parkin mediated UCH-L1 regulation may be a pathogenic mechanism contributing to neurodegeneration in human ARJP patients with parkin mutations."
25403879
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"Together, these results support that parkin promotes UCH-L1 degradation through the autophagylysosome pathway but not the proteasome pathway."
25403879
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"Parkin promotes UCH-L1 degradation through the autophagy-lysosome pathway."
25403879