The MRN complex in double‐strand break repair and telomere maintenance
Open accessAbstract
Genomes are subject to constant threat by damaging agents that generate DNA double‐strand breaks (DSBs). The ends of linear chromosomes need to be protected from DNA damage recognition and end‐joining, and this is achieved through protein–DNA complexes known as telomeres. The Mre11–Rad50–Nbs1 (MRN) complex plays important roles in detection and signaling of DSBs, as well as the repair pathways of homologous recombination (HR) and non‐homologous end‐joining (NHEJ). In addition, MRN associates with telomeres and contributes to their maintenance. Here, we provide an overview of MRN functions at DSBs, and examine its roles in telomere maintenance and dysfunction.
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Nbs1 is important to localize the MRN complex into the nucleus and to act as a regulatory and protein recruitment adaptor in the MRN complex.
“Nbs1 is important to localize the MRN complex into the nucleus and to act as a regulatory and protein recruitment adaptor in the MRN complex.33”
From Mdm2 inhibitors synergize with topoisomerase II inhibitors to induce p53-independent pancreatic cancer cell death (2013) · cites this paper as [33]
The MRN complex coordinates signaling to induce cellular responses such as cell cycle arrest and DNA repair.
“Moreover, it coordinates signaling to induce cellular responses like cell cycle arrest and repair of DNA.33”
From Mdm2 inhibitors synergize with topoisomerase II inhibitors to induce p53-independent pancreatic cancer cell death (2013) · cites this paper as [33]
The MRN complex is a central hub in the detection of DNA damage.
“The MRN complex is a central hub in the detection of DNA damage.”
From Mdm2 inhibitors synergize with topoisomerase II inhibitors to induce p53-independent pancreatic cancer cell death (2013) · cites this paper as [33]
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The MRE11 complex: starting from the ends
Stracker, T. H., & Petrini, J. H. J. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3047 · Cited by 734 · see citing works
DNA Repair Pathway Choices in CRISPR-Cas9-Mediated Genome Editing
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Insight into the mechanism of inhibition of adeno-associated virus by the Mre11/Rad50/Nbs1 complex
Lentz, T. B., & Samulski, R. J. (2015) · Journal of Virology · doi:10.1128/jvi.01990-14 · Cited by 48 · see citing works
Conradt, L., Henrich, A., Wirth, M., Reichert, M., Lesina, M., Algül, H., Schmid, R. M., Krämer, O. H., Saur, D., & Schneider, G. (2013) · International Journal of Cancer · doi:10.1002/ijc.27916 · Cited by 30 · see citing works
- Authors
- Lamarche, B. J., Orazio, N. I., & Weitzman, M. D.
- Affiliations
- Salk Institute for Biological Studies (US)
- Corresponding author
- Weitzman, Matthew D.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2010-07-22
- Volume
- 584
- Issue
- 17
- Pages
- 3682-3695
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- PMC
- PMC2946096
- OpenAlex
- W2028921845
- Cited by
- 446
- References
- 177
- Citations by year
- 2026: 11 · 2025: 22 · 2024: 23 · 2023: 17 · 2022: 40 · 2021: 51 · 2020: 35 · 2019: 33 · 2018: 34 · 2017: 34 · 2016: 32 · 2015: 22 · 2014: 28 · 2013: 16 · 2012: 16
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (AI067952, CA097093, AI051686)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- MRN complex, Mre11-Rad50-Nbs1, DNA double-strand break repair, telomere maintenance, homologous recombination, non-homologous end joining, telomere dysfunction, DNA damage response
- MeSH terms
- Animals, DNA Damage, DNA Repair, Humans, Mutation, Signal Transduction, Telomere, Genome, Sequence Deletion, Models, Animal, Nijmegen Breakage Syndrome, Mice, DNA Breaks, Double-Stranded
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