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DNA DAMAGE RESPONSE

Shieldin the ends for 53BP1

Nature Reviews Molecular Cell Biology volume 19, pages 346–347 (2018)Cite this article

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53BP1, RIF1 and REV7 have no known enzymatic activities, and no proteins were identified as their effectors. The authors used an ascorbate-peroxidase-based protein-proximity labelling approach in human cells to characterize the protein networks of 53BP1 and other DNA damage response factors, including the HDR factor BRCA1. The analyses identified direct and indirect interactions for the different factors and potential complexes that may constitute functional modules.

Intriguingly, 53BP1 interacted with an uncharacterized, ubiquitously-expressed 250-amino-acid protein. Affinity purification followed by mass spectroscopy showed that the protein directly interacts with REV7, and it was named REV7-interacting novel NHEJ regulator 1 (RINN1).

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Original article

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  • Chang, H.H.Y. et al. Non-homologous DNA end joining and alternative pathways to double-strand break repair. Nat. Rev. Mol. Cell Biol. 18, 495–506 (2017)

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  1. Nature Reviews Molecular Cell Biology http://www.nature.com/nrm/

    Eytan Zlotorynski

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  1. Eytan Zlotorynski
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Correspondence to Eytan Zlotorynski.

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Zlotorynski, E. Shieldin the ends for 53BP1. Nat Rev Mol Cell Biol 19, 346–347 (2018). https://doi.org/10.1038/s41580-018-0019-9

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