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The deubiquitylating enzyme USP15 regulates homologous recombination repair and cancer cell response to PARP inhibitors.

Abstract：

:Poly-(ADP-ribose) polymerase inhibitors (PARPi) selectively kill breast and ovarian cancers with defects in homologous recombination (HR) caused by BRCA1/2 mutations. There is also clinical evidence for the utility of PARPi in breast and ovarian cancers without BRCA mutations, but the underlying mechanism is not clear. Here, we report that the deubiquitylating enzyme USP15 affects cancer cell response to PARPi by regulating HR. Mechanistically, USP15 is recruited to DNA double-strand breaks (DSBs) by MDC1, which requires the FHA domain of MDC1 and phosphorylated Ser678 of USP15. Subsequently, USP15 deubiquitinates BARD1 BRCT domain, and promotes BARD1-HP1γ interaction, resulting in BRCA1/BARD1 retention at DSBs. USP15 knockout mice exhibit genomic instability in vivo. Furthermore, cancer-associated USP15 mutations, with decreased USP15-BARD1 interaction, increases PARP inhibitor sensitivity in cancer cells. Thus, our results identify a novel regulator of HR, which is a potential biomarker for therapeutic treatment using PARP inhibitors in cancers.

journal_name

Nat Commun

journal_title

Nature communications

authors

Peng Y,Liao Q,Tan W,Peng C,Hu Z,Chen Y,Li Z,Li J,Zhen B,Zhu W,Li X,Yao Y,Song Q,Liu C,Qi X,He F,Pei H

doi

10.1038/s41467-019-09232-8

subject

Has Abstract

pub_date

2019-03-15 00:00:00

pages

1224

issue

1

issn

2041-1723

pii

10.1038/s41467-019-09232-8

journal_volume

10

pub_type

杂志文章

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