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Article

Interaction between RNF8 and DYRK2 is required for the recruitment of DNA repair molecules to DNA double-strand breaks.

FEBS letters - 1 Mar 2017

Yamamoto Takenori, Taira Nihira Naoe, Yogosawa Satomi, Aoki Katsuhiko, Takeda Hiroyuki, Sawasaki Tatsuya, Yoshida Kiyotsugu

Abstract excerpt

The genome of eukaryotic cells is frequently exposed to damage by various genotoxins. Phosphorylation of histone H2AX at Serine 139 (γ-H2AX) is a hallmark of DNA damage. RNF8 monoubiquitinates γ-H2AX with the Lys63-linked ubiquitin chain to tether DNA repair molecules at DNA lesions. A high-throughput screening identified RNF8 as a binding partner of dual-specificity tyrosine phosphorylation-regulated kinase 2...

Read the complete abstract on PubMed

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Share to DNA Breaks, Double-Stranded
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Microscopy, Confocal

Share to Protein-Tyrosine Kinases

Share to Proto-Oncogene Proteins c-mdm2

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Source

Identifiers

PMID: 28194753
DOI: 10.1002/1873-3468.12596

Genes

DYRK2
RNF8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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