IndraLab

Statements


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"As ubiquitin chains are conjugated to the UBL domain [ 43 • ,44 ], one possibility might be that K6-linked ubiquitin conjugates somehow prevents binding of the RING0 domain to mitochondrial ubiquitin [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP30 antagonizes PINK1/Parkin-mediated mitochondrial autophagy [62,122]."

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"Here we report that USP30, a deubiquitinase localized to mitochondria, antagonizes mitophagy driven by the ubiquitin ligase parkin (also known as PARK2) and protein kinase PINK1, which are encoded by two genes associated with Parkinson 's disease."

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"One model consistent with this observation envisages that by suppressing basal ubiquitylation at mitochondria, USP30 may effectively limit PINK1 ubiquitin-substrate availability and the generation of pUb ' Parkin-receptor sites ', thus primarily influencing the initiation phase of mitophagy 86."

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"On the other hand, inhibition of USP30 expression or activity could allow cells to overcome the defects of PINK1 and Parkin, and restore the clearance of impaired mitochondria (Bingol et al., 2014)."

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"The investigation was performed in vitro system; However, additional experiments in FD animal models are necessary to validate the impact and mechanism of CHSGP on ICC mitophagy.The results of our stu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Loss or inhibition of USP30 can promote PINK1-dependent mitophagy."

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"USP30 Inhibits PINK1/Parkin-Dependent Mitophagy by Deubiquitinating Mitochondrial Proteins."

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"Our data showing that USP30 suppresses a PINK1 dependent component of basal mitophagy indicate a link between USP30 function and phospho-ubiquitin, the key substrate of PINK1 in mitophagy."

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"Additionally, USP30 activity can decrease the ubiquitin present on the OMM available for PINK1 to phosphorylate, setting a trigger threshold for PINK1/Parkin dependent mitophagy."

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"Strikingly USP30 knockdown invivo could rescue the PINK1 or Parkin -/- phenotypes in Drosophila, indicating that the inhibition of USP30 could be therapeutically advantageous in patients with equivalent null mutations in these genes [XREF_BIBR]."