IndraLab

Statements

USP1 deubiquitinates PCNA. 44 / 44
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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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"Review"
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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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"Significantly, we report that PCNA polyubiquitination is negatively regulated by USP1."
20353596
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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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"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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"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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"PCNA polyubiquitination, similar to PCNA monoubiquitination, is negatively regulated by USP1 [138,141]."
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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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"S4A, USP1 inhibited PCNA ubiquitination but not affected PCNA NEDDylation."
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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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"PCNA polyubiquitination, similar to PCNA monoubiquitination, is negatively regulated by USP1 [XREF_BIBR, XREF_BIBR]."
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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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"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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"Based on these findings it was proposed that monoubiquitination of PCNA is upregulated by the degradation or inactivation of USP1."
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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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"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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"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]"
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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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"The mono-ubiquitination of PCNA is usually reversed by USP1, however, USP1 does not cleave UbL73P chains (XREF_FIG)."
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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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"Deubiquitination of FANCD2, FANCI, and PCNA by USP1 is essential for DNA repair signalling."
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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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"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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"The USP1 and UAF1 complex also deubiquitinates PCNA-Ub, and deubiquitination requires the PCNA binding protein hELG1."
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"USP1 deubiquitinates PCNA and FANCD2 in cells."
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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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"USP1 also deubiquitinates the monoubiquinated form of proliferating cell nuclear antigen (PCNA) [XREF_BIBR]."
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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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"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 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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"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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"This decrease in USP1 activity allows PCNA ubiquitylation levels to increase and promote TLS [XREF_BIBR]."
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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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"USP1 modulates DNA replication polymerase choice and repair by deubiquitinating PCNA."
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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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"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."
27151298
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"Thus the timing of deubiquitination of PCNA by USP1 is still not clear."
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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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"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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"PCNA deubiquitination by USP1 [63,64] also likely regulates SHM, although its role has not been extensively analyzed.A major question that still remains concerning the MMR pathway in SHM is the identi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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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"ELG1 (enhanced level of genomic instability 1) interacts with the USP1 and UAF1 complex and supports USP1 mediated de-ubiquitination of PCNA [62]."
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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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