Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Open accessAbstract
In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear "leakiness" is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event.
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In senescent fibroblasts, mCherry was aggregated in the cytoplasm and colocalized with eGFP.
“In the senescent fibroblasts, mCherry was aggregated in the cytoplasm and colocalized with eGFP (Figure 1E–1G), consistent with a previous report [34, 35].”
From Chemically induced reprogramming to reverse cellular aging (2023) · cites this paper as [35]
The Results section (“Scaffold nucleoporins are not exchanged once inserted into the NE”; page unavailable) reports cytoplasmic accumulation and nuclear-envelope-associated aggregates of GFP-tagged nucleoporins in postmitotic myotubes. That supports the cited comparison to aggregation, but the paper does not report mCherry colocalizing with eGFP in senescent fibroblasts. (LLM, conf=0.84)
Experimental — accuracy not yet measuredIn neurons and astrocytes directly converted from fibroblasts of old humans, as well as old nematodes and rat brain tissue, the nuclear pore complex is deteriorated, leading to increased nuclear permeability and cytosolic protein aggregation.
“In neurons and astrocytes directly converted from fibroblasts of old humans, as well as old nematodes and rat brain tissue, the nuclear pore complex is deteriorated, leading to increased nuclear permeability and cytosolic protein aggregation [34–36].”
From Chemically induced reprogramming to reverse cellular aging (2023) · cites this paper as [35]
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Experimental — accuracy not yet measuredDisruption of NCC is a well-established effect of aging across species and is directly associated with ALS and FTD.
“Disruption of NCC is a well-established effect of aging across species and is directly associated with other diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD).”
From Chemically induced reprogramming to reverse cellular aging (2023) · cites this paper as [35]
The Results (page not provided) report age-related loss of the nuclear pore permeability barrier in C. elegans and rats, supporting the aging-across-species portion. The Discussion (page not provided) mentions Alzheimer’s and Parkinson’s disease but describes an association with defective pores as a possibility to investigate; it does not establish a direct association with ALS or FTD. (LLM, conf=0.88)
Experimental — accuracy not yet measuredA quantitative NCC assay was developed that can readily distinguish between young, old, and senescent cells.
“In this study, we developed and utilized novel screening methods including a quantitative nucleocytoplasmic compartmentalization assay (NCC) that can readily distinguish between young, old, and senescent cells [34, 35].”
From Chemically induced reprogramming to reverse cellular aging (2023) · cites this paper as [35]
The Experimental Procedures section on nuclear permeability (page unavailable) describes a quantified fluorescent-dextran assay comparing nuclei from young and old rats and worms. It does not describe an NCC assay or show that the assay distinguishes senescent cells. (LLM, conf=0.78)
Experimental — accuracy not yet measuredDeterioration of nucleocytoplasmic compartmentalization is one of the most well-conserved physiological hallmarks of aging.
“One of the most well-conserved physiological hallmarks of aging is deterioration of nucleocytoplasmic compartmentalization (NCC), which can be visualized as the leakage of nuclear proteins into the cytoplasm and failure of proteins to be imported into the nucleus [34, 35].”
From Chemically induced reprogramming to reverse cellular aging (2023) · cites this paper as [35]
The Introduction and Results report age-related loss of nuclear-pore selectivity in postmitotic cells, supporting deterioration of nucleocytoplasmic compartmentalization. The observed leakage is cytoplasmic tubulin entering the nucleus, not nuclear proteins entering the cytoplasm. The cited passages also do not establish failed nuclear import or that this is among the most well-conserved hallmarks of aging. (LLM, conf=0.88)
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- Authors
- D'Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. W.
- Affiliations
- Salk Institute for Biological Studies (US)
- Corresponding author
- Hetzer, Martin W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 136
- Issue
- 2
- Pages
- 284-295
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2805151
- OpenAlex
- W2091241169
- Cited by
- 565
- References
- 53
- Citations by year
- 2026: 29 · 2025: 32 · 2024: 34 · 2023: 36 · 2022: 40 · 2021: 38 · 2020: 44 · 2019: 35 · 2018: 36 · 2017: 31 · 2016: 31 · 2015: 29 · 2014: 24 · 2013: 20 · 2012: 25
- FWCI
- 14.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM057438)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- nuclear pore complex, nuclear integrity, aging, postmitotic cells, nucleoporins, Nup153, Nup50, oxidative damage, nuclear envelope, protein turnover
- MeSH terms
- Animals, Cell Nucleus, Mitosis, Down-Regulation, Caenorhabditis elegans, Nuclear Pore, Nuclear Pore Complex Proteins, Mice, Rats
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