IndraLab

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OTUB1 is hydroxylated. 24 / 24
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"The authors subsequently went on to demonstrate in detail, the consequences for FIH-dependent hydroxylation on OTUB1 ( Scholz et al., 2015 ) (a deubiquitinase important in linking IL-1β dependent sign[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26768963
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"Next, we analyzed whether IκBβ is hydroxylated by FIH via mass spectrometry (MS), because for OTUB1 the same asparagine residue that is involved in oxomer formation is also hydroxylated in monomeric OTUB1. xref We identified IκBß peptides containing four of the five asparagine residues."
38644795
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"Of note, the DMOG-dependent inhibition of OTUB1 hydroxylation was partly reversed by FIH overexpression when compared to the effect of DMOG without FIH overexpression ( xref )."
26752685
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"Expanding on their previous finding that OTUB1 is hydroxylated ( xref ), Scholz and colleagues determined the factor inhibiting HIF hydroxylates OTUB1 at N22 and that this restricts the OTUB1 interactome ( xref )."
30400005
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"Overall, these data led us to hypothesize that OTUB1 hydroxylation by FIH may be a link in the association of FIH with an alteration in cellular metabolism."
26752685
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"Mutation of the OTUB1 Hydroxylation Site Regulates its Interactome."
26752685
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"No difference was observed between maximally hydroxylated OTUB1 and minimally hydroxylated OTUB1 protein levels ( xref )."
26752685
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"Taken together, these data suggest the possibility that OTUB1 hydroxylation may at least in part provide a molecular explanation for some aspects of the observed phenotype in FIH-deficient mice."
26752685
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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."
26752685
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"In an attempt to investigate the implications of the hydroxylation of OTUB1 at this key hinge region, we found no impact of OTUB1 hydroxylation on OTUB1 protein levels or half-life ( xref )."
26752685
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"For example, hydroxylation of OTUB1 by factor inhibiting HIF (FIH) leads to a profound change in the interaction of OTUB1 with proteins important in cellular metabolism. [ xref ] This alteration of OTUB1 interactome affects OTUB1 localization and substrate accessibility."
33511009
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"We previously reported that the oxygen sensor FIH regulates cellular energy metabolism through hydroxylation of OTUB1 [ xref ]."
35163456
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"Moreover, oxygen-regulated factor inhibiting HIF (FIH) was found to hydroxylate the DUB OTUB1."
31706510
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"Although OTUB1 hydroxylation by FIH regulates metabolic processes in the cell [ xref ], a role of OTUB1 in activating the NF-κB pathway under hypoxic conditions has yet to be established."
28536364
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"Protein X signal intensity was proportional to OTUB1 protein levels, while mutation of the OTUB1 hydroxylation site (N22A) abrogated it ( xref B)."
31299612
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"Overall, these results demonstrate that mutations of the OTUB1 hydroxylation site and of its FIH interaction site affect FIH-OTUB1 HD levels and that both are necessary for optimal interaction and HD formation."
31299612
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"While OTUB1 enzymatic activity was dispensable for HD formation, the OTUB1 hydroxylation site as well as the FIH interaction site were necessary."
31299612
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"Possibly, HIF1AN’s impact on metabolism involves asparagine hydroxylation of the deubiquitinase OTUB1 that seems to suppress binding to many proteins related to metabolic processes [ xref ]."
31034925
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"Factor inhibiting HIF regulates OTUB1 deubiquitinase activity by catalyzing OTUB1 hydroxylation in an oxygen-dependent manner ( xref , xref )."
36822329
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"Among the oxygen sensors, 2OG‐dependent dioxygenases, such as prolyl hydroxylases (PHDs) and factor inhibiting HIF (FIH), are crucial in stabilizing HIF and influencing pathways related to oxygen availability, including NF‐κB. Proteomics studies have identified components of the NF‐κB pathway, such as p105, IκBα, and OTU domain‐containing ubiquitin aldehyde‐binding proteins 1 (OTUB1), as hydroxylation targets of FIH, linking oxygen sensing to NF‐κB regulation. xref , xref Although OTUB1 hydroxylation affects cellular metabolism, its direct involvement in hypoxia‐induced NF‐κB activation is yet to be fully understood."
39415849
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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 ]."
27005664
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"Hydroxylation of OTUB1 by FIH on asparagine residue N22 results in a restriction in its interactome, leading us to hypothesize a possible role for hydroxylation in substrate targeting."
26752685
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"2.6 OTUB1 asparagine hydroxylation."
27663420
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"Scholz et al . [ xref ] demonstrates a direct link between FIH-induced OTUB1 hydroxylation and cellular metabolism reprogramming, which may be important in human disease settings, especially in cancer where hypoxia serves as a hallmark and regulates cellular protein hydroxylation."
27663420