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OTUD1 deubiquitinates PRDX4. 3 / 3
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"We found OTUD1 selectively deubiquitinates PRDX4 during retranslocation from ER, thus protecting it from ERAD.PRDX4 is a critical component of the ER folding machinery where it mediates the formation of intra- and intermolecular disulfide bonds during oxidative protein folding ."
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"Mechanistically, OTUD1 deubiquitinates peroxiredoxin 4 (PRDX4), protecting it from endoplasmic reticulum (ER)-associated degradation."
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"Thus, we conclude that OTUD1 deubiquitinates PRDX4 and regulates its abundance, possibly by protecting it from degradation.To date, no activity of ubiquitin ligases was detected inside ER ."
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