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USP15 deubiquitinates PRKN. 10 / 10
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"Moreover, both USP15 and USP30 function indirectly, deubiquitinating substrates of PARKIN."

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"It is confirmed that USP15 antagonistically regulates the parkin-mediated mitophagy, but further investigation is required to determine whether the substrates of parkin related to other MOM proteins, [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP15 has been shown to deubiquitinate receptor-activated SMADs and TRIM25 and antagonize Parkin-mediated mitochondrial ubiquitination, and USP15 regulates the TGF-β pathway and is a key factor in glioblastoma pathogenesis (Eichhorn et al., 2012; Pauli et al., 2014; Inui et al., 2011)."

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"USP15 Deubiquitinates Parkin Substrates and Inhibits Mitophagy."

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"USP15 does not deubiquitylate Parkin under basal conditions or when cells are treated with mitochondrial depolarizing agents."

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"However, we found no evidence that USP15 deubiquitinates Parkin in basal conditions or after exposure to valinomycin (Fig. 5A and B)."

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"Similarly, the deubiquitinating enzymes USP15 [124], USP33 [63], and USP8 [125] have been shown to antagonize Parkin-mediated mitochondrial ubiquitination and mitophagy."

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"In contrast to USP8, USP15 was unable to deubiquitinate PARKIN; rather, USP15 exerts its effect by deubiquitinating mitochondrial substrates of PARKIN."

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"Thus, USP15 and USP30 both deubiquitinate substrates of PARKIN and oppose PARKIN function in mitophagy."

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"At present, the negative regulatory mechanisms against Parkin-mediated ubiquitination have been reported, with the discovery of several deubiquitinases including USP8, USP15 and USP30 that are able to cause the deubiquitination of Parkin and/or OMM proteins."