IndraLab

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FIH hydroxylates OTUB1. 5 / 5
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"These data provide a mechanistic link between FIH dependent hydroxylation of OTUB1 and alterations in cellular metabolism and contribute a further level of understanding to the vital link between cellular oxygen sensing mechanisms and the control of cellular metabolism."
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"Therefore, a possible contributory mechanism for the anti-inflammatory activity of hydroxylase inhibitors is through altered FIH dependent hydroxylation of OTUB1, leading to differential metabolism at inflamed sites."
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"In our study, we found that N22, the site of OTUB1 hydroxylation by FIH, is located in a region of the protein that may be key to determining its activity."
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"Although OTUB1 hydroxylation by FIH regulates metabolic processes in the cell [XREF_BIBR], a role of OTUB1 in activating the NF-kappaB pathway under hypoxic conditions has yet to be established."
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"The exception to this, is hydroxylation of OTUB1 by FIH, where mutation of the acceptor asparagine changes the interactome of OTUB1 and gives rises to metabolic changes in the cell [XREF_BIBR]."
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