IndraLab

Statements

USP15 binds BARD1. 17 / 17
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"USP15 interacts with BARD1 via its C-terminal region."
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"Furthermore, cancer-associated USP15 mutations, with decreased USP15-BARD1 interaction, increases PARP inhibitor sensitivity in cancer cells."
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"Interestingly, USP15–BARD1 interaction was increase after IR, HU, MMC, or CPT treatment (Fig.  xref )."
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"Moreover, USP15 C-terminal is mutated in breast cancer patients, disrupting USP15–BARD1 interaction and resulting in HR defect."
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"USP15 deletion mutant (deletion residues 740–981) abolished the binding of USP15 with BARD1."
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"As shown in Fig.  xref , endogenous USP15 and BARD1 associated with each other in cells."
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"More interestingly, patients carried USP15 mutations that disrupted USP15-BARD1 interaction, and the cancer cell is more sensitive to PARP inhibitor."
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"Since USP15 interacts with BARD1 and this interaction is important for HR, we hypothesized that BARD1 is the prime target of USP15."
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"Furthermore, the interaction between USP15 and BARD1 was confirmed by in vitro glutathione S -transferase (GST) pull-down assay (Supplementary Fig.  xref )."
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"Importantly, USP15–BARD1 interaction is essential for HR and cancer cell response to PARP inhibitor (Fig.  xref and Supplementary Fig.  xref )."
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"Since USP15 interacts with BARD1 and this interaction is important for HR, we hypothesized that BARD1 is the prime target of USP15."
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"USP15 interacts with BARD1 via its C-terminal region."
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"USP15 deletion mutant (deletion residues 740-981) abolished the binding of USP15 with BARD1."
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"At the molecular level, USP15 M861V/D967H disrupted USP15-BARD1 interaction and failed to deubiquitinate BARD1 at the BRCT domain (Fig.  xref )."
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"As USP15 affects BARD1 recruitment to DSBs, we next examined whether USP15 could interact with BARD1."
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"Furthermore, the interaction between USP15 and BARD1 was confirmed by in vitro glutathione S-transferase (GST) pull-down assay."
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"As USP15 affects BARD1 recruitment to DSBs, we next examined whether USP15 could interact with BARD1."
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