IndraLab

Statements

OTUD1 activates NFE2L2. 12 / 12
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"Taken together, these above observations indicate that OTUD1 stabilizes and activates NRF2 through its C320 catalytic residue and ETGE motif."
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"These collective findings promoted us to investigate the regulatory mechanism by which deubiquitinase OTUD1 activates NRF2 in the pathogenesis of hepatic I/R injury.Here, we have demonstrated that OTUD1 functions as a specific DUB for NRF2, leading to the stabilization and activation of the NRF2/ARE pathway, thereby results in the reduction of oxidative stress, apoptosis and inflammation in I/R-challenged liver."
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"Considering that OTUD1 possess DUB activity [28] and NRF2 activation is tightly regulated by deubiquitination [22], it is postulated that OTUD1 may activate NRF2 by removing ubiquitin chains from NRF2."
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"These collective findings promoted us to investigate the regulatory mechanism by which deubiquitinase OTUD1 activates NRF2 in the pathogenesis of hepatic I/R injury."
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"Keeping in line with the data, luciferase assay revealed that overexpression of OTUD1-WT markedly enhanced NRF2 luciferase activity."
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"Mechanistically, OTUD1 deubiquitinates and activates nuclear factor erythroid 2-related factor 2 (NRF2) through its catalytic site cysteine 320 residue and ETGE motif, thereby attenuating hepatic I/R injury."
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"Considering that OTUD1 possess DUB activity [ xref ] and NRF2 activation is tightly regulated by deubiquitination [ xref ], it is postulated that OTUD1 may activate NRF2 by removing ubiquitin chains from NRF2."
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"Mechanistically, OTUD1 deubiquitinates and activates nuclear factor erythroid 2-related factor 2 (NRF2) through its catalytic site cysteine 320 residue and ETGE motif, thereby attenuating hepatic I/R injury."
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"In short, OTUD1 prefers abolishing proteosome-mediated NRF2 degradation rather than modulating NRF2 function through removing K63 polyubiquitin scaffold.Due to its robust cytoprotective role in preventing oxidative stress and inflammation, NRF2 activation is considered a promising therapeutic strategy for numerous diseases characterized by oxidative stress [40]."
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"We utilized cycloheximide (CHX) to inhibit protein translation and observed that OTUD1 overexpression dramatically prolonged the half-life of NRF2 protein in AML12 cells (Fig. 4C), signifying its role in stabilizing NRF2."
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"Nucleocytoplasmic separation experiments showed that OTUD1 enhanced NRF2 nuclear accumulation (Fig. 4D)."
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"Collectively, this data supports that OTUD1 stabilizes and activates NRF2 by removing K11-, K27- and K48- linked ubiquitin chains from NRF2."
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