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OTUD5 binds UBR5. 35 / 40
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"UBR5-OTUD5 complex mitigates DNA replication fork stress."
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"UBR5-OTUD5 complex mitigates transcription-replication conflicts."
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"We hypothesized that the OTUD5-UBR5 complex may mitigate TRCs, based on our previous finding that the OTUD5-UBR5 complex regulates DNA double strand break (DSB)-induced transcription arrest, and that OTUD5-UBR5 proteins are present at replication forks (Figure 1G)."
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"UBR5 co-precipitates with OTUD5 (Figure xref ), and the purified recombinant OTUD5 and UBR5 proteins interact in vitro (Figure xref ; xref for western blot), suggesting that they interact directly."
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"PLA detected the interaction between UBR5 and OTUD5 at damaged chromatin in situ , and that the interaction spots partially coincide with the DNA DSB marker 53BP1 (Figure xref ), suggesting that at least a fraction of the interaction indeed occurs at damage (DSB) sites."
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"Previous studies report that OTUD5 interacts with UBR5, a HECT-type K48-linkage specific E3, in the regulation of DNA damage response and NF-κB signaling xref , xref ."
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"Mass spectrometry coupled to short interfering RNA (siRNA) screening of ubiquitinated proteins in Duba −/− Th17 cells revealed that DUBA directly bound and deubiquitinated UBR5 (Ubiquitin protein ligase E3 component n-recognin 5)."
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"We could confirm the interactions between OTUD5 and ARID1A/B, HDAC2, HCF1, and UBR5 by immunoblotting at the endogenous level in hES H1 cells (XREF_FIG)."
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"These results unequivocally suggest that both the UBR5–OTUD5 interaction and OTUD5–SPT16 interaction are necessary for transcriptional repression at the damaged chromatin."
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"To test our hypothesis, we first assessed whether there is any detectable interaction between OTUD5, UBR5, ATMIN and ATM."
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"Mapping analysis demonstrated that OTUD5 interacts with UBR5 through the N-terminal disordered tail region, and deleting the tail (17 amino acids) abrogated its ability to stabilize UBR5."
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"The OTUD5-UBR5 complex regulates FACT-mediated transcription at damaged chromatin."
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"When the either interaction-deficient OTUD5 mutant is expressed in OTUD5 KO cells, the cells are defective in arresting Pol II elongation and nascent RNA synthesis, underscoring the importance of the engagement of the UBR5–OTUD5 complex with SPT16 in transcription repression."
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"These data support a model, in which the OTUD5–UBR5 complex interacts with SPT16 and antagonizes its activity in facilitating the exchanges of new H2A molecules at the damaged chromatin."
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"We propose that repression of FACT activity by the OTUD5–UBR5 complex is crucial for generating a barrier for the Pol II from gaining access to DNA breakages, and relieving this barrier is necessary for the timely elongation of Pol II during recovery from damage."
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"Thus, our work propose that FACT is an important factor in this in cis regulation, and that FACT is subject to regulation by OTUD5–UBR5 complex for the non-lesion stalling of Pol II."
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"In addition, UBR5 interacts with DUBA, a negative regulator of IL-17 in T cells, to inhibit DUBA abundance in naïve T cells and thereby up-regulate IL-17, functioning to regulate the inflammatory response."
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"Despite our expectation that OTUD5 interacts directly only with UBR5 and interacts transiently and indirectly with ATMIN and/or ATM, thereby posing a challenge for detection, we readily detected an interaction of OTUD5 with all three endogenous proteins (UBR5, ATMIN and ATM) (Fig.  xref )."
39420004
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"PLA detected the interaction between UBR5 and OTUD5 at damaged chromatin in situ, and that the interaction spots partially coincide with the DNA DSB marker 53BP1 (Figure 2F), suggesting that at least a fraction of the interaction indeed occurs at damage (DSB) sites."
30508113
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"These data support a model, in which the OTUD5–UBR5 complex interacts with SPT16 and antagonizes its activity in facilitating the exchanges of new H2A molecules at the damaged chromatin."
30508113
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"We propose that repression of FACT activity by the OTUD5–UBR5 complex is crucial for generating a barrier for the Pol II from gaining access to DNA breakages, and relieving this barrier is necessary for the timely elongation of Pol II during recovery from damage.It is important to note that the mechanism of transcriptional arrest we describe is distinct from the direct stalling of Pol II by the lesions (e.g."
30508113
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"Thus, our work propose that FACT is an important factor in this in cis regulation, and that FACT is subject to regulation by OTUD5–UBR5 complex for the non-lesion stalling of Pol II.Our work leaves several open-ended questions; our data collectively suggest that OTUD5 and UBR5 repress FACT histone exchange activity, but how does this complex exactly achieve this?"
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"Since UBR5 can stably associate with OTUD5 , UBR5 may transiently ubiquitylate OTUD5 with K48-linked chains."
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"DUBA interacted with the ubiquitin ligase UBR5, which suppressed DUBA abundance in naive T cells."
25470037
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"Our prior data also demonstrated potential interaction between UBR5 and OTUD5, as both were part of the GPX4 complex (Fig.  xref )."
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"We previously showed that FACT-mediated transcription contributes to a recovery from a DNA double strand breaks (DSBs), and that this activity is antagonized by the OTUD5-UBR5 complex ( xref )."
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"UBR5-OTUD5 complex mitigates DNA replication fork stress."
37713620
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"UBR5-OTUD5 complex mitigates transcription-replication conflicts."
37713620
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"We hypothesized that the OTUD5-UBR5 complex may mitigate TRCs, based on our previous finding that the OTUD5-UBR5 complex regulates DNA double strand break (DSB)-induced transcription arrest, and that OTUD5-UBR5 proteins are present at replication forks (Figure xref )."
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"However, anti-SPT16 co-immunoprecipitation showed that the interaction with UBR5 and OTUD5 proteins is lost in the KI cells (Figure xref )."
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"DUBA interacted with the ubiquitin ligase UBR5, which suppressed DUBA abundance in naive T cells."
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"The OTUD5‐UBR5 axis contributes to DISC by preventing access of elongating RNAPII to break‐bearing genes."
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"DUBA interacts with and stabilizes the ubiquitin ligase UBR5 in activated T cells, and UBR5 catalyzes ubiquitination of RORγt in response to TGF-β and thereby suppresses Th17 differentiation."
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"First, OTUD5 interacts with UBR5 and represses RNA Pol II-mediated elongation and RNA synthesis."
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"We previously showed that FACT-mediated transcription contributes to a recovery from a DNA double strand breaks (DSBs), and that this activity is antagonized by the OTUD5-UBR5 complex (37)."
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