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UCHL3 deubiquitinates RAD51. 23 / 24
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"UCHL3 interacts with and deubiquitinates RAD51."
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"After DNA damages, UCHL3 is activated via phosphorylation by ATM and then deubiquitinates RAD51 promoting RAD51-BRCA2 interaction and proper HR repair [150]."
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"Reconstituting wild-type UCHL3 but not catalytically inactive UCHL3 (CA) reversed the increase in RAD51 ubiquitination induced by UCHL3 deficiency (Fig. 2E), suggesting that UCHL3 regulates RAD51 ubiquitination through its Ub protease activity.To determine whether UCHL3 directly deubiquitinates RAD51, we performed an in vitro deubiquitination assay."
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"Because UCHL3 promotes RAD51 deubiquitination following DNA damage, we further investigated whether and how UCHL3 itself is regulated following DNA damage."
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"Taken together, these results suggest that UCHL3 deubiquitinates RAD51 both in vitro and in vivo."
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"Collectively, these results suggest that UCHL3 promotes RAD51 deubiquitination following DNA damage."
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"Deubiquitination of RAD51 by UCHL3 is important for HR."
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"Following DNA damage, UCHL3 promotes RAD51 deubiquitination (Figs."
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"It is possible that RAD51 deubiquitination by UCHL3 is important for its recruitment to DSBs."
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"To directly test how RAD51 deubiquitination affects its binding to BRCA2, we deubiquitinated RAD51 by UCHL3 in vitro and examined its interaction with the BRCA2-BRC4 fragment."
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"These results suggested that deubiquitination of RAD51 by UCHL3 following DNA damage is important for the interaction between RAD51 and BRCA2.We next mapped potential ubiquitination sites of RAD51 that are regulated by UCHL3."
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"As shown in Figure 4B, loss of UCHL3 dramatically increased ubiquitination of wild-type RAD51 but not the 3KR (K56/57/63R) mutant with three N-terminal lysines mutated."
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"We next generated single mutations at these sites and found that a single mutation did not significantly affect RAD51 ubiquitination induced by UCHL3 deficiency (Fig. 4C)."
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"In response to DNA damage, UCHL3 is phosphorylated and activated by ATM, and activated UCHL3 positively regulates HR by deubiquitinating RAD51 to promote the BRCA2-RAD51 interaction ."
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"As shown in Figure 5H, RAD51 ubiquitination was dramatically decreased following IR treatment in cells reconstituted with wild-type UCHL3 but not in those reconstituted with the S75A mutant, suggesting that UCHL3 phosphorylation is important for UCHL3's deubiquitination of RAD51 following DNA damage."
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"Altogether, these in vitro results suggested that farrerol is an activator of UCHL3.Since a previous report indicated that UCHL3 deubiquitinates RAD51 to promote its interaction with BRCA2, thereby simulating its recruitment at DNA damage sites and enhancing HR repair , we examined whether farrerol promoted the deubiquitination of RAD51 in a UCHL3-dependent manner."
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"Both wild-type UCHL3 and the S75A mutant could deubiquitinate RAD51 in vitro, again suggesting a basal deubiquitination activity of UCHL3 that is not regulated by UCHL3 phosphorylation."
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"Since UCHL3 deubiquitinates RAD51 and regulates HR, we next investigated the role of UCHL3 in cancer."
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"Following DNA damage, a DUB, UCHL3, deubiquitinates RAD51 and promotes binding between RAD51 and BRCA2 and the recruitment of RAD51 to DSBs, which in turn facilitates HR."
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"UCHL3 deubiquitylates RAD51 to promote the interaction between RAD51 and BRCA2 and HR repair [121]."
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"found that UCHL3 deubiquitinates RAD51 and subsequently facilitates RAD51-BRCA2 interaction, which is critical for homologous recombination (HR) and contributes to therapeutic resistance in breast cancer."
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"RAD51 deubiquitination by UCHL3 was observed both in vitro and in cellulo and shown to be critical for BRCA2-RAD51 interaction, RAD51 recruitment to DSB sites, foci formation, as well as RAD51 mediated D-loop formation [XREF_BIBR]."
| PMC
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"Interestingly deubiquitylation of hRAD51 by UCHL3 at K57/58/64 promotes the hRAD51-BRCA2 interaction and is essential for HR [ 155 ]."
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