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RNF8/RNF168-dependent Lys63-linked polyubiquitination at sites of DNA double-strand breaks (DSBs) was originally regarded as the sole ubiquitin-signaling pathway involved in the DNA damage response (DDR). However, ubiquitin-dependent p97/VCP segregase activity and RNF8-dependent Lys48-linked polyubiquitin chains at DSB sites have recently been identified as components of an additional and parallel ubiquitin-signaling DDR pathway. This newly identified pathway is essential to spatiotemporal protein turnover and regulates both main branches of DSB repair, homologous recombination and nonhomologous end joining. In this report, the function of the RNF8/Lys48 polyubiquitin chains/p97 pathway is discussed in the context of DSB repair and p97 chromatin-related functions.

Original publication




Journal article


Cell Cycle

Publication Date





1062 - 1069


Adenosine Triphosphatases, BRCA1 Protein, Binding Sites, Cell Cycle, Cell Cycle Proteins, Chromatin, DNA Breaks, Double-Stranded, DNA Repair, DNA Replication, DNA-Binding Proteins, Enzyme Activation, Humans, Lysine, Models, Genetic, Proteasome Endopeptidase Complex, Protein Binding, Proteolysis, Signal Transduction, Substrate Specificity, Ubiquitin-Protein Ligases, Ubiquitination, Valosin Containing Protein