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USP30 deubiquitinates MFN2. 9 / 10
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"Inhibition of USP30 Promotes Mitophagy by Regulating Ubiquitination of MFN2 by Parkin to Attenuate Early Brain Injury After SAH."

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"Mfn2 can be ubiquitinated by Parkin and deubiquitinated by USP30 [ 35 , 36 ]."

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"In oxygen–glucose deprivation/reperfusion (OGDR) models, USP30 overexpression inhibits OGDR-induced ubiquitination and degradation of Mfn2 and reduces mitochondrial fragmentation [135]."

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"Inhibition of USP30 Promotes Ubiquitination of MFN2 by Parkin."

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"Henriques et al. showed that USP30 inhibition increased the ubiquitination of MFN2 and led to the extension of the mitochondrial network, while USP30 also depended on MFN2 to regulate mitochondrial morphology [39]."

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"However, contrary to our findings, Yue et al. found that USP30 mediated non-degradative ubiquitination of MFN2 [9]."

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"Specifically, studies performed in HeLa cells overexpressing c-Myc-tagged Ubiquitination Proteasome System (USP) demonstrated that S3 targets a mitochondria-localized deubiquitinase USP30, which mediates deubiquitination of MFN1 and MFN2 and regulates mitochondrial morphology."

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"Additionally, USP30 promotes mitochondrial fusion by deubiquitinating Mfn1 and Mfn2."

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"USP30 can also directly deubiquitinate MFN2 and TOMM20 to delay the recruitment of Parkin to mitochondria and subsequent mitophagy."