RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins

@article{Mailand2007RNF8UH,
  title={RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins},
  author={Niels Mailand and Simon Bekker-Jensen and Helene Faustrup and F. Melander and Jiri Bartek and Claudia Lukas and Jiri Lukas},
  journal={Cell},
  year={2007},
  volume={131},
  pages={887-900}
}

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References

SHOWING 1-10 OF 53 REFERENCES
Histone acetylation by Trrap–Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
TLDR
It is shown that the HAT cofactor Trrap and Tip60 HAT bind to the chromatin surrounding sites of DNA double-strand breaks (DSBs) in vivo, revealing that cells may use the same basic mechanism involving HAT complexes to regulate distinct cellular processes, such as transcription and DNA repair.
Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks
TLDR
It is proposed that subclassification of DSB regulators according to their residence sites provides a useful framework for understanding their involvement in diverse processes of genome surveillance.
BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair.
TLDR
An immunohistochemical approach is used to demonstrate that BRCA1 directed ligation of ubiquitin occurs during S-phase and in response to replication stress and DNA damage and is therefore likely to be a significant aspect of B RCA1 cellular activity.
The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response.
TLDR
It is shown that following ionizing radiation and treatment with DNA-damaging agents, RAP80 translocates to discrete nuclear foci that colocalize with those of gamma-H2AX and that RAP 80 can function as a substrate of the ataxia-telangiectasia mutated protein kinase in vitro, which phosphorylation is not required for the migration of R AP80 to IRIF.
Mdc1 couples DNA double‐strand break recognition by Nbs1 with its H2AX‐dependent chromatin retention
TLDR
Mdc1 functions as an H2AX‐dependent interaction platform enabling a switch from transient, Mdc1‐independent recruitment of Nbs1 to DSBs towards sustained, MDC1‐dependent interactions with the surrounding chromosomal microenvironment.
MDC1 is required for the intra-S-phase DNA damage checkpoint
TLDR
Findings reveal that MDC1-mediated focus formation by the MRE11 complex at sites of DNA damage is crucial for the efficient activation of the intra-S-phase checkpoint.
RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites
TLDR
Mutations affecting the BRCT domains of the breast cancer–associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs), implicating ubiquitin chain recognition and turnover in the BRCa1-mediated repair of DSBs.
Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1
TLDR
In vivo measurements identify Mdc1/NFBD1 as a key upstream determinant of 53BP1's interaction with DSBs from its dynamic assembly at the DSB sites through sustained retention within the D SB-flanking chromatin up to the recovery from the checkpoint.
Role of histone H2A ubiquitination in Polycomb silencing
TLDR
The purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A is reported, and it is linked to Polycomb silencing, which is important in regulating chromatin dynamics and transcription.
...
...