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PRKN binds USP8. 15 / 16
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"Specifically, S- persulfidation levels of the deubiquitinating enzyme USP8 were decreased in these mice, where NaSH exposures increased USP8 S- persulfidation and restored USP8/Parkin interactions fac[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Moreover, PARK2 interacts with the deubiquitinating enzyme USP8 that preferentially removes these K6-linked conjugates, thereby regulating the activity and function of PARK2 in the pathway."
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"Our results showed that hyperglycemia and hyperlipidemia decreased the translocation of parkin in the mitochondrial outer membrane and decreased the interaction between USP8 and parkin."
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"Our results showed that exogenous H 2 S could result in the S-sulfhydration of USP8 under hyperglycemia and hyperlipidemia, leading to the enhanced interaction of USP8 with parkin and the translocation of parkin into mitochondria."
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"Further, DTT inhibited the interaction of USP8 with parkin."
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"The association between parkin and USP8 is suggested to be via the CCCP-induced parkin translocation and DUB RNAi-based screening ( Durcan et al., 2014 )."
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"Consistent with previous reports that USP8 regulates Parkin-mediated mitophagy by removing K6-linked ubiquitin chains, which facilitates Parkin translocation to damaged mitochondria [ xref , xref ], USP8 binds to Parkin in osteoclasts and stabilizes it through deubiquitination-dependent mechanism."
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"Our results showed that the S-sulfhydration level of USP8 was obviously decreased in vivo and in vitro under hyperglycemia and hyperlipidemia, however, exogenous H 2 S could reverse this effect and promote USP8/parkin interaction."
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"To examine whether USP8 regulates osteoclast development via Parkin stabilization, we performed co-immunoprecipitation analysis in Raw264.7 cells, demonstrating the interaction between USP8 and Parkin (Fig.  xref A)."
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"The results showed that NaHS treatment increased the USP8/parkin interaction in db/db cardiac tissues (Fig. 5C)."
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"Our results showed that hyperglycemia and hyperlipidemia decreased the translocation of parkin in the mitochondrial outer membrane and decreased the interaction between USP8 and parkin."
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"Dithiothreitol, a reducing agent that reverses sulfhydration-mediated covalent modification, increased the ubiquitylation level of parkin, abolished the effects of exogenous H 2 S on USP8 deubiquitylation and suppressed the interaction of USP8 with parkin in neonatal rat cardiomyocytes treated with high glucose, oleate and palmitate."
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"In the diabetic heart, ubiquitin specific peptidase 8 (USP8) has been implicated: H 2 S was found to increase the association of parkin with USP8."
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"Our results showed that the effects of exogenous H 2 S on USP8 deubiquitylation and the interaction of USP8 with parkin were blocked with DTT treatment ( xref )."
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