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USP1 deubiquitinates PCNA. 78 / 79
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"Consistently, cells lacking Usp1, the enzyme that de-ubiquitinates PCNA exhibited increased TLS across a UV lesion and the cisplatin adduct."
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"Upon UV-light induced DNA damage, Usp1 is degraded so that PCNA becomes ubiquitylated XREF_BIBR, XREF_BIBR, suggesting that Usp1 deubiquitylates PCNA continuously in the absence of DNA damage XREF_BIBR."
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"Upon UV light induced DNA damage, Usp1 undergoes autocleavage, and PCNA therefore becomes ubiquitylated, suggesting that Usp1 continuously deubiquitylates PCNA in the absence of DNA damage."
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"USP1 also deubiquitinates Ub-PCNA, suggesting that it plays a role in regulating Ub-PCNA-mediated translesion synthesis (TLS) ( Huang et al., 2006 )."
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"Wild-type USP1 that is autocleavage-inactive (G670A, G671A) deubiquitinated Ub–PCNA subunits, whereas catalytically inactive USP1 (C90S) did not."
39145935
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"These findings demonstrate that ATAD5-N modulates Ub–PCNA deubiquitination process directly and is crucial for UAF1–USP1 to efficiently deubiquitinate Ub–PCNA."
39145935
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"PCNA polyubiquitination, similar to PCNA monoubiquitination, is negatively regulated by USP1 [XREF_BIBR, XREF_BIBR]."
25743599
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"During unperturbed replication, PCNA ubiquitination is limited by USP1, as evidenced by increased PCNA ubiquitination upon USP1 depletion (XREF_FIG)."
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"Deubiquitination of PCNA by USP1 was confirmed in vitro, and the specificity of the reaction was demonstrated by testing an irrelevant DUB enzyme and a catalytically inactive form of USP1.The investig[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"This is in contrast to UV mediated DNA damage whereby USP1 is degraded to enhance PCNA monoubiquitination, suggesting that alternate mechanisms inhibit USP1 activity in a time dependent manner (XREF_FIG)."
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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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"Finally, the deubiquitinase USP1 has been implicated in DNA damage response as it has been shown to deubiquitinate PCNA (139,140)."
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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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"Consistent with this, suppression of USP1 increases the level of mono-ubiquitinated PCNA in the absence of DNA damage during S phase [61], suggesting that USP1 suppresses PCNA mono-ubiquitination duri[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28666590
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"ELG1 (enhanced level of genomic instability 1) interacts with the USP1 and UAF1 complex and supports USP1 mediated de-ubiquitination of PCNA [62]."
28666590
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"The reversal of PCNA monoubiquitination by USP1 regulates TLS."
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"Overall, these findings argue that, by promoting PCNA de-ubiquitination, USP1 causes an increase in replication-associated ssDNA gaps which are subsequently converted into DSBs, potentially causing genomic instability."
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"S4A, USP1 inhibited PCNA ubiquitination but not affected PCNA NEDDylation."
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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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"Rad18, having a high affinity for ssDNA coated with RPA ( Davies et al., 2008 ), can bind the gaps and monoubiquitinates PCNA.PCNA is deubiquitinated by the protease USP1, and after UVC irradiation, U[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP1 deubiquitinates PCNA and FANCD2 in cells."
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"Deubiquitylation of PCNA by Usp1 or conversion of monoubiquitylation to polyubiquitylation prevents polymerase switching and repair of the lesion must rely on other mechanisms."
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"Two recent studies revealed that a major function of USP1 and its partner UAF1 is to suppress sporadic monubiquitination of PCNA during normal DNA replication [XREF_BIBR, XREF_BIBR]."
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"Moreover, we show that this suppression reflects the USP1 de-ubiquitination activity towards PCNA rather than other substrates, since it depends on RAD18-mediated PCNA ubiquitination."
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"USP1 also deubiquitinates the monoubiquinated form of proliferating cell nuclear antigen (PCNA) [XREF_BIBR]."
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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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"[88] USP1 deubiquitinates PCNA—an important component of the trans-lesions synthesis (TLS) repair pathway."
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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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"Knockdown of USP1 induces aberrant PCNA monoubiquitylation, enhanced recruitment of error-prone TLS polymerases and increased mutagenesis levels in human cells ."
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"In sensitive cells, USP1 inhibition induces aberrant PCNA mono- and polyubiquitination followed by PCNA protein loss."
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"For instance, USP1 loss leads to aberrant PCNA monoubiquitylation, resulting in enhanced recruitment of error-prone TLS polymerases and destabilized replication forks in cells lacking the homologous recombination factor BRCA1 [31]."
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"USP1 modulates DNA replication polymerase choice and repair by deubiquitinating PCNA."
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"This decrease in USP1 activity allows PCNA ubiquitylation levels to increase and promote TLS [XREF_BIBR]."
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"USP1 also deubiquitinates PCNA [96], another key player in the rescue of stalled replication forks, as well as in DNA crosslink repair [97,98]."
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"The mono-ubiquitination of PCNA is usually reversed by USP1, however, USP1 does not cleave UbL73P chains (XREF_FIG)."
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"While USP1 constitutively deubiquitinates PCNA to prevent the abnormal engagement of TLS polymerases, notably Pol κ, USP1 undergoes its own autocleavage and degradation upon UV damage, allowing for PCNA monoubiquitination to be elevated [90,91]."
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"While the USP1 autocleavage mutant is still able to deubiquitinate PCNA, its expression results in increased fork stalling and premature fork termination."
37445667
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"In the translesion synthesis pathway, USP1 deubiquitinates proliferating cell nuclear antigen (PCNA) in order to prevent recruitment of low-fidelity polymerases and thereby preserve DNA integrity [74][MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Suppression of USP1 increased the basal level of PCNA mono-ubiquitination in unirradiated cells, which is produced during DNA replication ( Huang et al., 2006 )."
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"In mammals, deubiquitination of PCNA is mediated by the deubiquitinase USP1 in conjunction with its interacting partner UAF1 in the absence of DNA damage [62–64] ."
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"USP1 also negatively regulates polyubiquitination in mammals and therefore may participate in deubiquitination of PCNA during recovery after DNA repair by this pathway [77] ."
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"However, suppression of USP7 and also USP1 clearly increased H 2 O 2 -induced PCNA mono-ubiquitination, indicating that some fraction of these enzymes is still active in H 2 O 2 -treated cells and cap[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In undamaged cells, suppression of USP1 significantly promoted mono-ubiquitination of PCNA at 16 and 20 hr, but not at 8 hr, after release ( Figures 3 C and 3D, lanes 13–15)."
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"Suppression of USP1 promoted UV-induced PCNA mono-ubiquitination at 16 and 20 hr, but not at 8 hr, after release ( Figure 3 C; compare lanes 16–18 with lanes 4–6), again suggesting that USP1 suppresse[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Suppression of USP1 increased H 2 O 2 -induced PCNA mono-ubiquitination to a greater extent at 16 and 20 hr than at 8 hr after release ( Figure 3 D, lanes 16–18), relative to control cells (lanes 4–6)[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Deubiquitination of FANCD2, FANCI, and PCNA by USP1 is essential for DNA repair signalling."
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"Moreover, poly-ubiquitinated PCNA became readily detectable when Usp1 was removed (XREF_FIG), suggesting that Usp1 limits the poly-ubiquitination of PCNA in human cells."
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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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"Efficient TLS polymerase filling of ssDNA gaps also requires USP1-dependent deubiquitination of Ub-PCNA."
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"The USP1 and UAF1 complex also deubiquitinates PCNA-Ub, and deubiquitination requires the PCNA binding protein hELG1."
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"In this study, we show that USP1 can suppress ssDNA gaps in BRCA1-deficient tumor cells by deubiquitinating its key substrate, PCNA."
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"Recently, PCNA deubiquitylation by the USP1 and UAF1 complex in conjunction with ELG1, which directs the USP1-UAF1 to ubiquitin-PCNA, has emerged as an important regulatory mechanism of damage bypass."
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"USP1 also deubiquitinates PCNA (proliferating cell nuclear antigen), an important component of the trans-lesions synthesis (TLS) repair pathway ( Huang et al., 2006 )."
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"The converse was also true: H 2 O 2 -induced mono-ubiquitination of PCNA was increased by suppression of either USP1 or USP7, but elevation of the H 2 O 2 -induced mutation frequency was observed only[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Once this process is complete, USP1 is required for deubiquitination of PCNA and reversion to canonical DNA replication."
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"Whereas Rad6/Rad18 E2 conjugate/E3 ligase cause PCNA monoubiquitination, Usp1 and Usp7 cause PCNA deubiquitination with some difference in case of HU (Niimi et al, 2008; Fox et al, 2011)."
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"Another piece of evidence for a tight coordination between the two pathways is the notion that the isopeptidase USP1 mediates deubiquitylation of both PCNA and the ID complex."
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"Significantly, we report that PCNA polyubiquitination is negatively regulated by USP1."
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"USP1, which is localized at the replication fork, deubiquitinates PCNA and thus stabilizes the fork."
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"In 2006 Huang et al., were the first to reveal that USP1 negatively regulates monoubiquitination of PCNA in the absence of DNA damage in order to control TLS [XREF_BIBR]."
20353596
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"USP1 deubiquitinates PCNA, thus contributing to prevent unscheduled recruitment of error-prone TLS DNA polymerases [XREF_BIBR]."
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"An interesting mechanistic facet of DNA damage bypass concerns the regulation of PCNA deubiquitylation, which in human cells is mediated by the isopeptidase USP1 in complex with its co-factor, UAF1."
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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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"Deubiquitinase USP1 is the most investigated deubiquitinating enzyme of PCNA-Ub, surprisingly USP1 is degraded through autocleavage upon DNA damage induction by UV, but not mitomycin C (MMC), methyl methanesulfonate (MMS) or hydroxylurea (HU) (54,55)."
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"PCNA deubiquitination by USP1 [XREF_BIBR, XREF_BIBR] also likely regulates SHM, although its role has not been extensively analyzed."
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"USP1 deubiquitinates PCNA, enabling the replication fork to resume its high-fidelity replication."
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"A potential mechanism for this might employ the deubiquitinating enzyme Usp1, which can reverse monoubiquitination of PCNA ( Huang et al., 2006 )."
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"Later studies showed that USP1 also deubiquitinates proliferating cell nuclear antigen (PCNA) and Fanconi anemia complementation group I (FANCI)."
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"USP1 deubiquitylates mono-ubiquitylated PCNA, which inhibits DNA polymerases recruiting in the absence of DNA damage, resulting in regulating DNA repair."
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"Based on these findings it was proposed that monoubiquitination of PCNA is upregulated by the degradation or inactivation of USP1."
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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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"USP1 is an important regulator of the DNA damage response, deubiquitinating mono-ubiquitinated FANCD2/I and PCNA [6, 8, 9]."
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"This raises the possibility that in certain circumstances, cells might resort to “on the fly” lesion bypass in the context of replication forks, though such a co-replicative mechanism would be constit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Deubiquitination of PCNA by USP1 can also limit the access of TLS Polkappa to the replication fork and ensure the low mutation frequency of DNA replication."
23797609
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"For example, USP1 deubiquitylates mono-ubiquitylated PCNA, which inhibits recruitment of DNA polymerases in the absence of DNA damage, and thereby leads to regulated DNA repair."
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"Thus the timing of deubiquitination of PCNA by USP1 is still not clear."
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"PCNA deubiquitination by USP1 was one of the first mechanisms described as a negative regulator of eukaroytic TLS, and since then, several other mechanisms have been described."
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"Thus, deubiquitination of PCNA, normally deubiquitinated by cellular USP1, by the viral DUB can disrupt repair of DNA damage by compromising recruitment of TLS polymerase to stalled replication forks."
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