Genomic instability in laminopathy-based premature aging
Abstract
Premature aging syndromes often result from mutations in nuclear proteins involved in the maintenance of genomic integrity. Lamin A is a major component of the nuclear lamina and nuclear skeleton. Truncation in lamin A causes Hutchinson-Gilford progerial syndrome (HGPS), a severe form of early-onset premature aging. Lack of functional Zmpste24, a metalloproteinase responsible for the maturation of prelamin A, also results in progeroid phenotypes in mice and humans. We found that Zmpste24-deficient mouse embryonic fibroblasts (MEFs) show increased DNA damage and chromosome aberrations and are more sensitive to DNA-damaging agents. Bone marrow cells isolated from Zmpste24-/- mice show increased aneuploidy and the mice are more sensitive to DNA-damaging agents. Recruitment of p53 binding protein 1 (53BP1) and Rad51 to sites of DNA lesion is impaired in Zmpste24-/- MEFs and in HGPS fibroblasts, resulting in delayed checkpoint response and defective DNA repair. Wild-type MEFs ectopically expressing unprocessible prelamin A show similar defects in checkpoint response and DNA repair. Our results indicate that unprocessed prelamin A and truncated lamin A act dominant negatively to perturb DNA damage response and repair, resulting in genomic instability which might contribute to laminopathy-based premature aging.
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The gene responsible for the progeroid Hutchinson-Gilford syndrome has been identified, and there is evidence that its product helps to maintain nuclear architecture and to regulate genomic stability.
“the gene responsible for the progeroid Hutchinson-Gilford syndrome has also been identified, and there is evidence that its product helps to maintain nuclear architecture and to regulate genomic stability 43”
From The common biology of cancer and ageing (2007) · cites this paper as [43]
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- Authors
- Liu, B., Wang, J., Chan, K. M., Tjia, W. M., Deng, W., Guan, X., Huang, J.-D., Li, K. M., Chau, P. Y., Chen, D. J., Pei, D., Pendas, A. M., Cadiñanos, J., López-Otín, C., Tse, H. F., Hutchison, C., Chen, J., Cao, Y., Cheah, K. S. E., Tryggvason, K., & Zhou, Z.
- Affiliations
- University of Hong Kong (HK)
- University of California San Diego (US)
- The University of Texas Southwestern Medical Center (US)
- University of Minnesota (US)
- Universidad de Oviedo (ES)
- Durham University (GB)
- Mayo Clinic (US)
- Karolinska Institutet (SE)
- Corresponding author
- Zhou, Zhongjun
- ORCID
- Venue
- Nature Medicine
- Published
- 2005-06-26
- Volume
- 11
- Issue
- 7
- Pages
- 780-785
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W2053206914
- Semantic Scholar
- 11c8c8f2e30401376ed6a80c0f6ad3567f9a30e0
- Cited by
- 650
- References
- 25
- Citations by year
- 2026: 14 · 2025: 20 · 2024: 20 · 2023: 22 · 2022: 25 · 2021: 27 · 2020: 38 · 2019: 28 · 2018: 44 · 2017: 33 · 2016: 36 · 2015: 40 · 2014: 33 · 2013: 34 · 2012: 24
- FWCI
- 13.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Keywords
- laminopathies, premature aging, Hutchinson-Gilford progeria syndrome, ZMPSTE24, lamin A, genomic instability, DNA damage response, DNA repair, 53BP1, RAD51, aneuploidy, chromosomal abnormalities, dominant negative effect
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, Animals, Bone Marrow Cells, Chromosomal Proteins, Non-Histone, Chromosome Aberrations, DNA, DNA Damage, DNA Repair, DNA-Binding Proteins, Fibroblasts, Gamma Rays, Histones, Humans, Membrane Proteins, Metalloendopeptidases, Mice, Mutant Strains, Nuclear Proteins, Phosphoproteins, Protein Precursors, Cellular Senescence, Aging, Premature, Lamin Type A, Genomic Instability, Intracellular Signaling Peptides and Proteins, Rad51 Recombinase, Mice
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