IndraLab

Statements

USP8 activates Ubiquitin. 7 / 7
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"And USP8 catalyzes ubiquitin removal from both Lys48 linkage and Lys63 linkage polyubiquitination chains."
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"These results suggest that the CCL5 gene is activated in an NF-κB–dependent manner in USP8-depleted cells.Since USP8 depletion causes the accumulation of K63 ubiquitin chains on endosomes, we hypothesized that the K63 ubiquitin signals directly activate NF-κB via ubiquitin decoders."
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"Moreover, P5091 inhibits USP7-, but not USP2- or USP8 mediated cleavage of poly K48 linked ubiquitin chains (visualized by the presence or absence of mono-ubiquitin) (XREF_SUPPLEMENTARY)."
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"USP8 enhances mitophagy by removing lysine-6-linked ubiquitin from parkin, promoting its turnover [XREF_BIBR]."
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"USP8 is also directly connected to Parkin-mediated mitophagy by controlling the removal of K6-linked ubiquitin from Parkin."
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"71 In contrast to PAR2, USP8 (or AMSH) does not impact CXCR4 ubiquitination but instead modulates the ubiquitin status of ESCRT-0 that is ubiquitinated by the E3 ligase AIP4, 23 reinforcing the idea that ubiquitination of the transport machinery represents an important regulatory event in GPCR trafficking."
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"K63 ubiquitin accumulation on early endosomes in USP8-depleted cells was rescued by the add-back of wild-type (WT) USP8, but not the catalytically inactive C786A mutant, in a deubiquitinating activity-dependent manner (Fig. S1 C)."
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