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USP1 deubiquitinates FANCD2. 58 / 60
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"USP1 influences accumulation of the Fanconi anaemia core complex at DNA damage sites and deubiquitylates FANCD2–FANCI in a cell cycle-dependent manner ."
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"Interestingly, the opposite effect (DNA promoting USP1‐UAF1‐mediated FANCD2 deubiquitination) has been reported in a study utilising a ~60% FANCD2‐ubiquitinated ID2 complex produced with the aid of a 64‐mer single‐stranded DNA (Liang et al, 2019)."
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"Interestingly, the recently identified deubiquitinating enzyme, USP1, negatively regulates both FANCD2 and PCNA monoubiquitination, suggesting an interaction between these seemingly parallel DNA damag[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP1 deubiquitinates both ub-FANCD2 [XREF_BIBR] and ub-FANCI [XREF_BIBR], thus reverting the critical event in the activation of the FA pathway."
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"The USP1 and UAF1 complex deubiquitylates FANCD2 and FANCI."
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"The UAF1 and USP1 complex deubiquitinates FANCD2 during execution of the Fanconi anemia DNA damage response pathway."
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"Finally, FANCD2 is deubiquitinated by the USP1 and UAF1 deubiquitinating enzyme complex [XREF_BIBR, XREF_BIBR]."
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"In addition to the monoubiquitination of FANCD2, deubiquitination of FANCD2 by deubiquitination enzyme USP1 is known to be required for ICL repair."
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"Finally, FANCD2-Ub and PCNA-Ub are coordinately deubiquitinated by the same deubiquitinating (DUB) enzyme complex, USP1 and UAF1 43."
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"However, after the overexpression of SERPINB3, the expression level of USP1 was increased, which could accelerate the deubiquitination of FANCD2–FANCI during ICLs repair."
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"FANCD2 deubiquitination by USP1, is also required for the FA pathway to function properly."
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"How USP1 eventually deubiquitinates the FANCD2 and FANCI complex following the completion of the DNA repair is still a question."
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"FANCD2 is deubiquitinated by USP1 once DNA repair is complete."
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"The ubiquitylation of both the FANCD2 and FANCI components is important to prevent the deubiquitylation of FANCD2 by the deubiquitinase USP1 and its binding partner UAF1 while it is DNA bound, as these cannot bind to the altered confirmation of monoubiquitylated FANCI, and thus cannot act on either subunit [16]."
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"The USP1/UAF1 complex deubiquitinates the Fanconi anemia protein FANCD2, thereby promoting homologous recombination and DNA cross-link repair."
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"When DNA repair mediated by the FA pathway is completed, the deubiquitinase USP1 reverses the monoubiquitination of FANCD2 [118]."
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"Similarly, USP1, which plays an important role in DNA repair by specifically deubiquitylating FANCI/FANCD2 (I-D2), relies on UAF1 for allosteric activation and substrate recognition ( Cohn et al., 200[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Inhibition of USP1 increases monoubiquitination of both FANCD2 and FANCI, indicating further coordinate regulation at this level as well."
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"Lastly, FANCD2 is deubiquitinated by USP1 and UAF1 complex to terminate the FA pathway."
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"When the DNA crosslink has been repaired, the USP1 and UAF1 deubiquitinating enzyme complex deubiquitinates FANCD2, causing disassembly of the DNA repair complex, and completion of the DNA repair process."
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"For example, USP1 deubiquitinates two critical DNA repair proteins, FANCD2 and PCNA, and is therefore involved in Fanconi leukemia XREF_BIBR, XREF_BIBR; USP9x deubiquitinates and stabilizes the pro survival protein MCL1, and a correlation between USP9x expression and MCL1 levels was reported in human follicular lymphomas and diffuse large B-cell lymphomas 84; USP37 is a deubiquitinase regulating cell cycle by deubiquitinating cyclin A 85 and c-MYC 86."
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"USP1 combined with USP1-associated factor 1 (UAF1) deubiquitinates PCNA or FANCD2 during DNA repair process such as interstrand cross-link (ICL) repair, homologous recombination (HR) repair, and translesion DNA synthesis (TLS) [87]."
| PMC
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"In addition, since DUBs have poor substrate specificity in vitro, it is difficult to obtain direct evidence for deubiquitination of FANCD2 by USP1 (Mason et al., 2004) ."
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"Upon DNA damage, USP1 is downregulated by transcriptional shut-off [86], perhaps to facilitate FANCD2 mono-ubiquitination."
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"More recent evidence suggests that a later deubiquitination of FANCD2 and FANCI by USP1 and UAF1 might be required for efficient foci assembly and HR mediated repair (J. Kim and A. D'Andrea, unpublished observation)."
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"This indicates that FANCD2 must be coordinately monoubiquitylated by the FA core complex and deubiquitylated by USP1 for efficient assembly of the protein into nuclear complexes to facilitate DNA repair."
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"The observation that FANCD2 monoubiquitination, which is also deubiquitinated by USP1, was normal in RAD51 knock down cells (XREF_FIG, lane 5 and 6) further supports this idea."
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"USP1 deubiquitinates PCNA and FANCD2 in cells."
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"In the Fanconi anemia pathway, USP1 deubiquitinates FANCD2 and FANCI, two components of the Fanconi anemia complex, in order to facilitate DNA repair."
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"USP1 protein alone was unable to deubiquitinate Ub-FANCD2 ( Figure 5 B, lane 2)."
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"However, cells lacking USP1, the DUB that negatively regulates FANCD2 ubiquitylation, are as sensitive to DNA crosslinking agents as FA cells [48-50]."
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"Previous studies have shown that USP1 deubiquitylates mono-ubiquitinated PCNA (ub-PCNA) and mono-ubiquitinated FANCD2 (ub-FANCD2) in response to replication stress due to DNA damage during DNA replication (4, 5, 41)."
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"We have previously shown that USP1, in complex with its stimulatory binding partner, UAF1, deubiquitinates the Fanconi Anemia (FA) proteins, FANCD2 and FANCI."
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"The activated FA pathway must be inactivated for completion and recycling of the functional pathway, and this event is regulated by the USP1 and UAF1 deubiquitinating enzyme complex, which deubiquitinates FANCD2 and FANCI."
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"Surprisingly, depletion of UBE2M did not reduce the FANCD2 monoubiquitination that is up-regulated by USP1 depletion (XREF_SUPPLEMENTARY), suggesting that the Nedd8 inhibition specifically abrogates FANCD2 monoubiquitination that is induced by exogenous DNA damage."
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"USP1 deubiquitinates ub-FANCD2 (Nijman et al., 2005) and ubFANCI (Sims et al., 2007), thereby restoring FA key events in pathway activation."
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"The exact role of deubiquitination of PCNA and FANCD2 by USP1 and UAF1 in human DNA damage response remains to be elucidated."
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"Mono-ubiquitylation of FANCD2 is reversed by USP1, a member of the protease family of de-ubiquitylating enzymes (DUBs) after the completion of repair [XREF_BIBR, XREF_BIBR]."
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"USP1 deubiquitylates FANCD2 which is included in the repair of DNA crosslinks."
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"The ubiquitylation activity of the FA core complex is provided by the FANCL subunit that encodes a PHD and RING containing Ub-ligase [7], whereas de-ubiquitylation of FANCD2 following ICL repair is me[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Usp1 deubiquitinates FANCD2 and FANCI in the Falconi anemia pathway, promoting DNA repair."
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"Deubiquitination of FANCD2, FANCI, and PCNA by USP1 is essential for DNA repair signalling."
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"For instance, it has been discovered that USP1-associated factor 1 (UAF1) and ubiquitin-specific peptidase 1 (USP1) deubiquitinate the proteins FANCD2, FANCI, and PCNA to control DDR."
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"A growing number of substrate-specific mammalian DUBs involved in tumorigenesis are continually being revealed such as USP1 and USP9X, which deubiquitinate FANCD2 and β-catenin, respectively ( Nijman [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Deubiquitination of FANCD2 and FANCI by USP1 in complex with UAF1 is also important for FA pathway function."
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"When the repair process is completed, the FANCD2 and FANCI complex is deubiquitylated and dissociated from the repaired ICL site by the USP1 and UAF1 complex and is then released from the DNA [XREF_BIBR]."
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"The deubiquitination of FANCD2 and FANCI by the UAF1 and USP1 deubiquitinating enzyme complex appears to be required for the completion of the repair process [XREF_BIBR - XREF_BIBR]."
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"The USP1 and UAF1 deubiquitinase complex deubiquitinates FANCD2 and reverses the FA pathway activation [XREF_BIBR]."
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"Subsequently, USP1 deubiquitinates FANCD2 to recycle FANCD2 and promote S phase exit [26]."
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"USP1 is well defined in its role in deubiquitinating monoubiquitylated PCNA [36] and Fanconi anemia pathways proteins, FANCD2 and FANCI [31, 32], to regulate the DNA damage response."
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"Deubiquitination of FANCD2 and FANCI proteins by the multisubunit protein complex USP1 and UAF1 is required for the completion of the FA pathway."
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"The USP1 and UAF1 complex deubiquitinates the Fanconi anemia protein FANCD2, thereby promoting homologous recombination and DNA cross-link repair."
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"Finally, USP1 deubiquitinates and inactivates two components of DNA repair mechanisms : FANCD2 (a component of the Fanconi Anemia pathway) XREF_BIBR, XREF_BIBR and PCNA XREF_BIBR."
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"USP1 deubiquitylates FancD2-Ub, and USP3 is thought to act on uH2A."
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"Conversely, mice deficient in Usp1, the protease which deubiquitinates Fancd2, have elevated cellular levels of Fancd2-Ub and are resistant to Ras induced squamous cell cancers."
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"Additionally, FANCD2 is regulated by the ATM and ATR kinases, is deubiquitinated by the deubiquitinating enzyme USP1, and turns off the FA pathway."
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"For example, USP1 deubiquitinates FANCD2/FANCI or PCNA to prevent the recruitment of interstrand crosslink repair proteins and translesion DNA polymerase to inhibit DNA repair; USP7 regulates lung squamous cell carcinoma cell proliferation through MEK/ERK signaling by deubiquitinates the Raf-1 [175,176]."
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"The USP1 and UAF1 complex deubiquitylates the Fanconi anemia protein FANCD2, which promotes homologous recombination (HR) and DNA cross-link repair."
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