The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Nuclear Tau, a Key Player in Neuronal DNA Protection
Open accessAbstract
Tau, a neuronal protein involved in neurodegenerative disorders such as Alzheimer disease, which is primarily described as a microtubule-associated protein, has also been observed in the nuclei of neuronal and non-neuronal cells. However, the function of the nuclear form of Tau in neurons has not yet been elucidated. In this work, we demonstrate that acute oxidative stress and mild heat stress (HS) induce the accumulation of dephosphorylated Tau in neuronal nuclei. Using chromatin immunoprecipitation assays, we demonstrate that the capacity of endogenous Tau to interact with neuronal DNA increased following HS. Comet assays performed on both wild-type and Tau-deficient neuronal cultures showed that Tau fully protected neuronal genomic DNA against HS-induced damage. Interestingly, HS-induced DNA damage observed in Tau-deficient cells was completely rescued after the overexpression of human Tau targeted to the nucleus. These results highlight a novel role for nuclear Tau as a key player in early stress response.
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“In particular, intranuclear tau is thought to bind to chromatin and stabilize it in response to cellular stressors such heat [149].”
From DNA repair deficiency and senescence in concussed professional athletes involved in contact sports (2019) · cites this paper as [149]
In the citing paper
“prevents DNA damage by oxidative stress 94, 106”
From Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome (2016) · cites this paper as [94]
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Citations
Cites
Single cell gel/comet assay: Guidelines for in vitro and in vivo genetic toxicology testing
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A protein factor essential for microtubule assembly
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Self-citationThe distribution of tau in the mammalian central nervous system.
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Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport
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I will survive: DNA protection in bacterial spores
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Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.
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Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA
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Items 401–420 of 420
Neurotoxicité précoce et mécanismes de neuroprotection dans des modèles poisson‐zèbre de tauopathies
Barbereau, C. (2020) · theses.fr (ABES) · doi:10.70675/dfe1802ez70f2z4da6zb3e5z63d1de7a429c
Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau
Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc
Caractérisation d'anticorps à domaine unique dirigés contre la protéine Tau
Danis, C. (2018) · theses.fr (ABES) · doi:10.70675/c783a062zb57bz4024z85d0z509baaed8a1b
“Des études réalisées sur des cultures neuronales et des 26 modèles de souris déficientes en Tau (KO-Tau) ont montré que Tau joue un rôle majeur dans la protection des dommages à l’ARN et à l’ADN (Sultan et al., 2011; Violet et al., 2014).”
BackgroundInfluentialAltered neuronal activity in the hippocampal CA3 region in an in vitro model of tauopathy
Goncalves, A. (2020) · theses.fr (ABES) · doi:10.70675/b42db6dez88a0z4a14z93eez8f51d19d46f5
Denéchaud, M. (2022) · theses.fr (ABES) · doi:10.70675/623e7224z0cb0z47b1z8a22z549acf553ac0
Yatoui, D. (2022) · theses.fr (ABES) · doi:10.70675/e3620ccez2ea7z43f2za0dcz257a72021b17
Castelot, R. (2024) · theses.fr (ABES) · doi:10.70675/c2a7ce1ez8caaz4593zbb3azae8add8055b5
Role of T-cell immunity in the pathophysiology of Alzheimer’s disease and other Tauopathies
Matta, K. (2024) · theses.fr (ABES) · doi:10.70675/cea4fe5ez67c3z4445z92f7z39af62ba059b
Astrocytes dysfunction in tauopathies
Augustin, E. (2023) · theses.fr (ABES) · doi:10.70675/a6b6a2f4zff42z4987z9ca0z62aca30c291c
Clemente, E., Sivasubramanian, R., Kordes, S., Bhatia, P., Hans, R., Vogel, S., Baumann, M., Klebl, B., & Sterneckert, J. L. (2026) · Cells · doi:10.3390/cells15131228
“Although, tau’s best studied function is its binding to neuronal microtubules, increasing evidence suggest that tau also has nuclear functions, including regulation of ribosomal RNA transcription, chromatin structure, and DNA damage [26–28].”
Metal Binding to Tau Protein: Physiological and Pathological Relevance
Quintanar, L., Juarez-Romero, G. U., & Lopez-Herrera, G. R. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00323
López-Aviña, Y. I., Ríos‐Castro, E., Rodríguez‐Cruz, F., Mendoza-Franco, G., Vega, B. C., Boucard, A. A., Luna‐Arias, J. P., Basurto‐Islas, G., & García‐Sierra, F. (2026) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2026.151567
Cottingham, K., Goodarzi, N., Fries, D., Lirushie, G., & Hall, H. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1851916
“Tau protein has also been shown to localize to the neuronal nucleus, where it can form DNA-protein complexes (Greenwood and Johnson, 1995; Hua et al., 2003; Sultan et al., 2011; Qi et al., 2015).”
Altered Membrane Protein Abundance in the Cerebral Cortex of the JNPL3 Mouse Model of Tauopathy
Petralla, S., Hyvärinen, J., Gynther, M., Afonin, A., Lehtonen, M., Auriola, S., Panayotova, M., Kanninen, K. M., Fricker, G., & Puris, E. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00679
Silvestri, F., Bronzato, E., Scambi, I., Arietti, V., Sacchetto, L., Mariotti, R., Zanusso, G., Bongianni, M., & Turano, E. (2026) · Cells · doi:10.3390/cells15191824
“Tau has been detected in the nuclei of both neuronal and non-neuronal cells, where it contributes to DNA protection [40].”
Tau phosphorylation from neuronal adaptation to Alzheimer’s disease
Trouvé, R., Verstreken, P., & Hoekstra, M. M. (2026) · Neuron · doi:10.1016/j.neuron.2026.08.032
Metadata
- Authors
- Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., Colin, M., Bonnefoy, E., Buée, L., & Galas, M.-C.
- Affiliations
- Inserm (FR)
- Institut Pasteur de Lille (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Galas, Marie-Christine
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 286
- Issue
- 6
- Pages
- 4566-4575
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3039398
- OpenAlex
- W2155048015
- Cited by
- 421
- References
- 54
- Citations by year
- 2026: 24 · 2025: 16 · 2024: 21 · 2023: 31 · 2022: 29 · 2021: 44 · 2020: 39 · 2019: 24 · 2018: 48 · 2017: 27 · 2016: 23 · 2015: 25 · 2014: 26 · 2013: 18 · 2012: 16
- FWCI
- 9.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission (200611)
- Agence Nationale de la Recherche
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- heat stress, oxidative stress, DNA damage, neurodegeneration, Alzheimer's disease, microtubule-associated proteins, stress response
- MeSH terms
- Alzheimer Disease, Animals, Cell Nucleus, Cells, Cultured, DNA, Humans, Neurons, Phosphorylation, tau Proteins, Mice, Knockout, Heat-Shock Response, Mice
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