IndraLab

Statements


USP30 activates PRKN. 10 / 10
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"USP30 knockdown also increases the ubiquitination level on multiple Parkin substrates, thus confirming that USP30 antagonizes Parkin function."

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"Although SILAC provides a rigorous way for performing quantification, other studies used label-free quantification to examine targeted mitochondrial outer membrane ubiquitylation by PARKIN in the presence or absence of the mitochondrial deubiquitylating enzyme USP30, leading to the identification of a dozen mitochondrial PARKIN targets that are regulated by USP30 (see below)."

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"Nevertheless, deletion of USP30 from cells with endogenous Parkin only results in a modest effect on mitophagic flux, and Parkin can rapidly overcome USP30’s activity to allow maximal activation of the Parkin dependent mitophagy ."

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"More specifically, USP30 has been reported to mediate Parkin and PINK1-dependent mitophagy following the acute depolarization of the mitochondria [9] via the deubiquitylating Parkin substrates in the mitochondria [10]."

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"Knockdown of USP30 rescues the defective mitophagy caused by pathogenic mutations in parkin and improves mitochondrial integrity in parkin- or PINK1 deficient flies."

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"Silencing USP30 alleviates d-gal-induced mitochondrial damage and consequently suppresses myocardial cell senescence by activating Parkin."

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"Although SILAC provides a rigorous way for performing quantification, other studies used label-free quantification to examine targeted mitochondrial outer membrane ubiquitylation by PARKIN in the pres[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"These results demonstrated that USP30 could promote d-gal-induced mitochondrial damage and cell senescence through antagonizing Parkin."

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"Knockdown of the Drosophila homologs of USP15 (CG8334, hereafter called dUSP15) and USP30 (CG3016, hereafter dUSP30) largely rescues the mitochondrial defects of parkin deficient fly muscle in vivo."

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"Knockdown of the mitochondrial deubiquitinase, USP30, rescues mitophagy defects and disease in flies with pathogenic mutations in Parkin, suggesting a potential role for the inhibition of DUBs that target selective autophagy E3 ligases in the treatment of Parkinson 's and other diseases."