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USP13 deubiquitinates UIMC1. 24 / 24
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"USP13 can deubiquitinate RAP80 (receptor-associated protein 80) and promote the recruitment of the RAP80-BRCA1 complex to damage sites, fine-tuning the DNA repair system ."
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"These results suggest that deubiquitination of RAP80 by USP13 following DNA damage facilitates the binding between RAP80 and K63- linked polyubiquitin chain."
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"Deubiquitination of RAP80 by USP13 plays an important role in the ability of RAP80 to bind polyubiquitin, which is important for RAP80 recruitment and DDR."
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"Our results suggest that USP13 deubiquitinates RAP80 following DNA damage, which in turn facilitates RAP80 recruitment to DSBs."
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"USP13, in turn, deubiquitinates RAP80 and promotes RAP80 recruitment and proper DDR."
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"USP13 interacts with and deubiquitinates RAP80."
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"USP13 deubiquitinates receptor associated protein 80 (RAP80) and promotes DNA damage response."
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"USP13 deubiquitinates RAP80, regulating RAP80-BRCA1 foci formation (55)."
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"Since USP13 deubiquitinates RAP80 and regulates DDR, we next examined the role of USP13 in cancer."
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"Also, USP13 interacts to and deubiquitylates receptor-associated protein 80 (RAP80) following DNA damage to activate its ability, promoting DNA-damage responses ."
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"For example, deubiquitination of RAP80 by USP13 facilitates the interaction between RAP80 and polyubiquitin chain and is important for RAP80-BRCA1 foci formation and DNA repair [117]."
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"Also, USP13 interacts with and deubiquitylates RAP80 to activate its function ."
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"<span class="match term0">USP13</span>, in turn, deubiquitinates <span class="match term1">RAP80</span> and promotes <span class="match term1">RAP80</span> recruitment and proper DDR."
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"In addition, USP13 specific inhibitor, Spautin-1, significantly enhanced RAP80 ubiquitination in control but not USP13 deficient cells (XREF_FIG)."
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"We found that following DNA damage, a deubiquitinase, USP13, deubiquitinates RAP80 and promotes binding between RAP80 and K63 linked polyubiquitin chains, which is important for the recruitment of the RAP80 and BRCA1 complex to DSBs to facilitate DDR."
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"RAP80 deubiquitinated by USP13 promotes DDR through BRCA1."
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"Next, we performed an in vitro deubiquitination assay to further confirm that USP13 directly deubiquitinates RAP80."
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"Taken together, these results suggest that USP13 deubiquitinates RAP80 both in vitro and in vivo."
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"25,26 Mechanistically, USP13 deubiquitinates RAP80 and promotes BRCA1 recruitment to DSBs, whereas UCH-L3 eliminates the polyubiquitin chains of RAD51 and facilitates RAD51–BRCA2 binding."
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"Deubiquitination of RAP80 by USP13 is important for DDR."
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"The interaction between RAP80 and the K63-linked polyubiquitin chain is increased when RAP80 is deubiquitinated by USP13, which is crucial for its recruitment to DNA damage sites and the formation of the RAP80-BRCA1 complex."
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"We demonstrated that polyubiquitination of RAP80 blocks its interaction with polyubiquitin chain and deubiquitination of RAP80 by USP13 facilitate the interaction between RAP80 and polyubiquitin chain."
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"Consistent with this, we found that RAP80 ubiquitination decreases following DNA damage (XREF_FIG and XREF_SUPPLEMENTARY), suggesting that USP13 promotes RAP80 deubiquitination following DNA damage."
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"Together with results showing USP13 is important for DDR and RAP80 localization at the sites of DNA damage, we hypothesized that RAP80 ubiquitination is inhibitory of its function, and deubiquitination of RAP80 by USP13 following DNA damage promotes RAP80 function in the DDR pathway."
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