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Article

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.

Nature - 1 Mar 2020

Suskiewicz Marcin J, Zobel Florian, Ogden Tom E H, Fontana Pietro, Ariza Antonio, Yang Ji-Chun, Zhu Kang, Bracken Lily, Hawthorne William J, Ahel Dragana, Neuhaus David, Ahel Ivan

Abstract excerpt

The anti-cancer drug target poly(ADP-ribose) polymerase 1 (PARP1) and its close homologue, PARP2, are early responders to DNA damage in human cells1,2. After binding to genomic lesions, these enzymes use NAD+ to modify numerous proteins with mono- and poly(ADP-ribose) signals that are important for the subsequent decompaction of chromatin and the recruitment of repair factors3,4. These post-translational...

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Identifiers

PMID: 32028527
DOI: 10.1038/s41586-020-2013-6
PMCID: PMC7104379

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HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.PMID 32028527Read ↗

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Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesionsSemantic proximity Read ↗

Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1Semantic proximity Read ↗

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