Author: Lyudmila Kovalchuke; Eugene V. Mosharov; Oren A. Levy; Lloyd A. Greene
Title: Stress-induced phospho-ubiquitin formation causes parkin degradation Document date: 2018_12_5
ID: ceepyyxj_54
Snippet: Additionally, our results support the findings of others that parkin can be degraded proteasomally [15] , [92] , [120] [121] [122] . The latter and additional studies [98] , [123] [124] [125] [126] [127] suggested that proteasomal parkin degradation is mediated by autoubiquitination, but this possibility was not directly tested. Our observation that catalytically inactive parkin was not protected from L-DOPA-induced loss indicates that parkin's p.....
Document: Additionally, our results support the findings of others that parkin can be degraded proteasomally [15] , [92] , [120] [121] [122] . The latter and additional studies [98] , [123] [124] [125] [126] [127] suggested that proteasomal parkin degradation is mediated by autoubiquitination, but this possibility was not directly tested. Our observation that catalytically inactive parkin was not protected from L-DOPA-induced loss indicates that parkin's proteasomal degradation downstream of stressinduced phospho-Ub binding is not due to autoubiquitination, as this only occurs in cis [98] . This finding is contrary to a model proposed to explain depolarization-induced parkin loss [40] , but is consistent with the finding that parkin autoubiquitination appears to protect it from degradation [36] .
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