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- W2047507923 abstract "Depolarized mitochondria are degraded via mitophagy in a process that depends on the Parkinson's disease gene products PINK1 and Parkin. This is accompanied by ubiquitination of several mitochondrial substrates. The roles of E2 ubiquitin-conjugating enzymes (UBE2) in mitophagy are poorly understood. Here we investigate a set of UBE2 enzymes that may regulate Parkin-mediated mitophagy. Knockdown of the E2 enzymes UBE2N, UBE2L3 or UBE2D2/3 significantly reduced autophagic clearance of depolarized mitochondria. However, this did not interfere with mitochondrial PINK1 stabilization and Parkin translocation. UBE2N knockdown prevented specifically K63-linked ubiquitination at mitochondrial sites. Nevertheless, poly-ubiquitin and p62 were still found on mitochondria after individual UBE2 knockdown. Knockdown of all three UBE2s together significantly reduced the mitochondrial poly-ubiquitination and p62 recruitment. Moreover, reduced ubiquitination of mitofusins, mitochondrial import receptor subunits TOM20 and TOM70, the voltage-dependent anion channel protein 1, and of Parkin was observed in cells silenced for all three UBE2s. The Parkin active site mutant C431S failed to ubiquitinate these mitochondrial substrates even in the presence of UBE2s. We conclude that UBE2N, UBE2L3 and UBE2D2/3 synergistically contribute to Parkin-mediated mitophagy." @default.
- W2047507923 created "2016-06-24" @default.
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- W2047507923 date "2014-01-01" @default.
- W2047507923 modified "2023-10-09" @default.
- W2047507923 title "UBE2N, UBE2L3 and UBE2D2/3 ubiquitin-conjugating enzymes are essential for parkin-dependent mitophagy" @default.
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- W2047507923 doi "https://doi.org/10.1242/jcs.146035" @default.
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