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Statements

USP4 binds RBBP8. 52 / 54
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"To identify the regions of USP4 that are responsible for the USP4-CtIP interaction, we generated deletion mutants of USP4 ( Figure 1 C)."
26387952
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"Our results revealed that USP4 interacts with CtIP and USP4-CtIP interaction is important for HR."
26387952
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"Of note, USP4 can deubiquitinate itself, and this autodeubiquitination function is crucial for the USP4-CtIP interaction, which occurs in HR ( xref ; xref )."
33681193
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"As shown in Figure 1 B, endogenous USP4 and CtIP interact with each other in cells."
26387952
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"Wijnhoven et al. revealed that the human deubiquitylase USP4 promotes homologous recombination, DNA end-resection, and CtIP recruitment and that USP4 interacts with CtIP and MRN."
26455393
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"In light of the above findings, we tested whether USP4 might physically interact with CtIP and/or MRN."
26455393
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No evidence text available
26455393
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"Because it was reported that USP4 interacts with CtIP but does not affect the latter’s ubiquitination level xref , we chose USP52 as the candidate DUB for CtIP."
33097710
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"USP4 interacts with the retinoblastoma binding protein 8 (CtIP, also known as RBBP8) and the MRE11RAD50-NBS1 (MRN) complex [XREF_BIBR, XREF_BIBR]."
30831436
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"Deletion of USP4 insert domain (residues 572-775) abolished the binding of USP4 with CtIP."
26387952
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"These papers have reported that USP4 interacts with MRN complex and CtIP dependently on its catalytic activity."
28764946
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"As USP4 directly interacts with CtIP, we also checked CtIP foci formation in USP4 depleted cells."
26387952
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"Because USP4 autodeubiquitination did not affect its levels, the next question we asked was whether USP4 autodeubiquitination could affect USP4-CtIP interaction."
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"These are consistent with our results; CtIP N-terminal could interact with USP4, and this interaction is essential for DNA end resection."
26387952
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"These results indicate that the USP4-CtIP interaction is required for its function in HR."
26387952
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"USP4 interacts with CtIP and MRN via the C-terminal insert domain (residues 572-773) and intact catalytic domain of USP4, respectively."
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"Mechanistically, USP4 interacts with CtIP and MRN via a specific, conserved region and the catalytic domain of USP4, respectively, and regulates CtIP recruitment to sites of DNA damage."
26387952
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"USP4 interacts with both CtIP and the MRN complex via a specific conserved region on USP4 and the catalytic domain of USP4, respectively, to promote the recruitment of the DNA end-resection factor CtIP to dsDNA break sites [ xref ]."
29641431
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"We hypothesized that USP4-CtIP interaction is required for CtIP recruitment to the DNA damage sites."
26387952
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No evidence text available
26455393
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"Of note, the interaction between USP4 and the DNA endonuclease CtIP (RDDP8), critical to DSB end resection in xref ; xref ), represents a postWGD neofunctionalization."
28177072
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"During the course of our studies, we observed that mutating theUSP4 catalytic cysteine to alanine (C311A) to render USP4 enzymatically inactive (" catalytic-dead " [CD]), almost totally abrogated its interactions with CtIP and MRN (XREF_FIG A; note that binding of USP4 to CtIP and RAD50 was not abrogated by the DNA intercalating agent ethidium bromide (EtBr), suggesting that interaction was not mediated by DNA bridging."
26455393
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"USP4 interacts with the retinoblastoma binding protein 8 (CtIP, also known as RBBP8) and the MRE11RAD50-NBS1 (MRN) complex [ xref , xref ]."
30831436
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"We and others report that USP4 interacts with CtIP and the MRE11-RAD50-NBS1 (MRN) complex and is required for CtIP recruitment to DNA damage sites and DNA end resection."
27940552
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"Additionally, we establish that USP4 interacts with CtIP and the MRN complex via its C-terminal insert domain and that these interactions are subject to a USP4 auto-regulatory deubiquitylation mechanism."
26455393
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"We did the coIP experiment after DNase treatment; this result indicated that CtIP-USP4 interaction was not bridged by DNA."
26387952
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"More importantly, USP4 ubiquitination can block USP4-CtIP interaction, whereas the USP4CA mutant could not mediate its autodeubiquitination, and sustained ubiquitination of USP4 would block its intera[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP4, for example, interacts directly with end resection factors CtIP and MRN [172], USP21 deubiquitinates and stabilizes BRCA2 to promote RAD51 binding and successful HR [173], and USP10 deubiquitinates and stabilizes p53 to promote its nuclear localization and apoptosis in response to DSBs [174]."
32708614
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"USP4 interacts with CtIP and regulates the recruitment of CtIP to DNA damage sites through its deubiquitylating enzyme activity ( xref )."
29244158
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"Here, we report that USP4 interacts with both MRN complex and CtIP, which is a positive regulator of DNA end resection, thus promoting HR.Both the C terminus and the N terminus of CtIP protein are req[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26387952
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No evidence text available
26387952
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"As USP4 directly interacts with CtIP, we also checked CtIP foci formation in USP4-depleted cells."
26387952
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"Mechanistically, USP4 interacts with CtIP and MRN via a specific, conserved region and the catalytic domain of USP4, respectively, and regulates CtIP recruitment to sites of DNA damage."
26387952
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No evidence text available
26387952
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"We set out to detangle the DUB network and distinguish redundancy that results from postduplicative conservation of interaction domains from neofunctionalization events, such as the WGD-derived USP4-CtIP interaction in DSB repair."
28177072
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"In addition, USP4 interacts with MRN and CtIP promotes the interaction between these proteins [ xref , xref ]."
32570875
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"Previous study showed that CtIP interacts with the MRE11-RAD50-NBS1 (MRN) complex and USP4 which is required for CtIP recruitment to DNA damage sites."
27940552
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"These are consistent with our results; CtIP N-terminal could interact with USP4, and this interaction is essential for DNA end resection."
26387952
reach
"Wealso report that USP4 interacts with CtIP and the MRE11-RAD50-NBS1 (MRN) complex and is required for CtIP recruitment to DNA damage sites."
26455393
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"They both demonstrated that USP4 interacts with CtIP and MRN and regulates the recruitment of CtIP to DSBs."
27602047
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"As shown in Figure 7 B, USP4 catalytic activity is essential for the USP4-CtIP interaction."
26387952
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"We also could not exclude other mechanisms; for example, there might be other factors that help the deubiquitinated USP4 interact with CtIP."
26387952
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No evidence text available
26387952
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"USP4 interacts with CtIP and regulates the recruitment of CtIP to DNA damage sites through its deubiquitylating enzyme activity."
29244158
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No evidence text available
26387952
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"These results indicate that the deubiquitylating enzyme activity of USP4 is required for its function in HR.Our results revealed that USP4 interacts with CtIP and USP4-CtIP interaction is important fo[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26387952
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"Because USP4 interacts with the N-terminal of CtIP through its insert domain, CtIP N-terminal is essential for its foci formation and depletion of USP4 decreased CtIP foci formation."
26387952
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"They both demonstrated that USP4 interacts with CtIP and MRN and regulates the recruitment of CtIP to DSBs."
27602047
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"This result suggests that USP4 promotes USP4-CtIP interaction specifically through its deubiquitinase activity and likely through its autodeubiquitination."
26387952
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"USP4 interacts with CtIP and MRN via the C-terminal insert domain (residues 572–773) and intact catalytic domain of USP4, respectively."
26387952
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"USP4-CtIP interaction is a little increased after IR treatment, but in the USP4CA mutant cells, USP4-CtIP interaction is almost gone, even in IR-treated cells."
26387952
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"Deletion of USP4 insert domain (residues 572–775) abolished the binding of USP4 with CtIP."
26387952