PARP1-specific inhibitor displays PARP1-detrapping activity

The successful use of PARP inhibitors against primarily homologous recombination-deficient tumors relies on their ability to inhibit the catalytic activity of PARP1 and PARP2, leading to their retention at sites of DNA damage, known as PARP "trapping." Different PARP inhibitors vary in their trapping ability and thus in their resulting toxicity. Here, we develop an inducible complementation system for the expression of tagged PARP1 variants to assess the impact of different mutations in the PARP1 catalytic site on ADP-ribosylation (ADPr) activity, trapping, and cell survival. Testing these cell lines for their behavior and sensitivity to different PARP inhibitors, we find that saruparib, a first-in-class PARP1-specific inhibitor, promotes the release of certain PARP1 catalytic mutants and resistance to this inhibitor. We also characterize a PARP1 catalytic mutant with intact mono(ADP-ribosyl)ation activity but devoid of poly(ADP-ribosyl)ation, enabling us to demonstrate a significant contribution of mono(ADP-ribosyl)ation toward PARP1 release from sites of DNA damage.

Authors

Institutions

Publication Details

Journal
Cell Reports
Published
2026-05-01
DOI
https://doi.org/10.1016/j.celrep.2026.117350
Primary Topic
PARP inhibition in cancer therapy
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

PARP1-specific inhibitor displays PARP1-detrapping activity

Domagoj Baretić, Chatrin Chatrin, Kira Schützenhofer, Michael D. R. Simmons et al.
Cell Reports
PARP inhibition in cancer therapy
article

PARP1-specific inhibitor displays PARP1-detrapping activity

Domagoj Baretić, Chatrin Chatrin, Kira Schützenhofer, Michael D. R. Simmons, Rebecca Smith, Ellen Laker, Kyle Tsang, Marcin J. Suskiewicz, Ivan Ahel, Florian F.H. Zobel
article en

Abstract

The successful use of PARP inhibitors against primarily homologous recombination-deficient tumors relies on their ability to inhibit the catalytic activity of PARP1 and PARP2, leading to their retention at sites of DNA damage, known as PARP "trapping." Different PARP inhibitors vary in their trapping ability and thus in their resulting toxicity. Here, we develop an inducible complementation system for the expression of tagged PARP1 variants to assess the impact of different mutations in the PARP1 catalytic site on ADP-ribosylation (ADPr) activity, trapping, and cell survival. Testing these cell lines for their behavior and sensitivity to different PARP inhibitors, we find that saruparib, a first-in-class PARP1-specific inhibitor, promotes the release of certain PARP1 catalytic mutants and resistance to this inhibitor. We also characterize a PARP1 catalytic mutant with intact mono(ADP-ribosyl)ation activity but devoid of poly(ADP-ribosyl)ation, enabling us to demonstrate a significant contribution of mono(ADP-ribosyl)ation toward PARP1 release from sites of DNA damage.

Cell ReportsVol. 45(5)
Centre National de la Recherche Scientifique (FR), University of Oxford (GB), Centre de Biophysique Moléculaire (FR)
Wellcome Trust, Cancer Research UK, Biotechnology and Biological Sciences Research Council
Openalex Percentile: Top 10%
PARP inhibition in cancer therapy
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.