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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Single cell gel/comet assay: Guidelines for in vitro and in vivo genetic toxicology testing
Tice, R. R., Agurell, E., Anderson, D. C., Burlinson, B., Hartmann, A., Kobayashi, H., Miyamae, Y., Rojas, E., Ryu, J., & Sasaki, Y. F. (2000) · Environmental and Molecular Mutagenesis · doi:10.1002/(sici)1098-2280(2000)35:3 · Cited by 4,885
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142
Self-citationThe distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588
Olive, P. L., Banáth, J. P., Durand, R. E., & Banáth, J. P. (1990) · Radiation Research · doi:10.2307/3577587 · Cited by 1,095
Olive, P. L., Banáth, J. P., & Durand, R. E. (2012) · Radiation Research · doi:10.1667/rrav04.1 · Cited by 1,031
Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport
Terry, L. J., Shows, E. B., & Wente, S. R. (2007) · Science · doi:10.1126/science.1142204 · Cited by 543
I will survive: DNA protection in bacterial spores
Setlow, P. (2007) · Trends in Microbiology · doi:10.1016/j.tim.2007.02.004 · Cited by 466
Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.
Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E. M., & Mandelkow, E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.12.1887 · Cited by 340
Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA
Брусков, В. И. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.6.1354 · Cited by 307
Flagged first, then by citations
Research works printed but not linked: 1
- Daniel, 2008, BBA, 1783, 1003
Cited by
Sorted by citations
Items 201–300 of 420
Neuropathology of Aging in Cats and its Similarities to Human Alzheimer’s Disease
Sordo, L., Martini, A. C., Houston, E. F., Head, E., & Gunn-Moore, D. A. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.684607 · Cited by 26
“These studies have shown that there is a significant dephosphorylation of cytoplasmic tau and an increase in nuclear tau immediately after inducing stress; whereas the opposite was observed after 24 h, with an increase in cytoplasmic tau phosphorylation and a decrease in nuclear tau (Sultan et al., 2011).”
BackgroundInfluentialThe Structure Biology of Tau and Clue for Aggregation Inhibitor Design
Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 27
Nuclear Tau, p53 and Pin1 Regulate PARN-Mediated Deadenylation and Gene Expression
Baquero, J., Varriano, S., Ordonez, M., Kuczaj, P., Murphy, M. R., Aruggoda, G., Lundine, D., Morozova, V., Makki, A. E.-H., Alonso, A. D. C., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00242 · Cited by 26
“In the nucleus, tau phosphorylation affects its ability to bind and protect DNA during heat stress (Sultan et al., 2011; Qi et al., 2015) and, as shown here, to regulate PARN-mediated deadenylation and steady-state levels of target mRNAs.”
BackgroundInfluentialCerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside
Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25
“Additionally, aggregated tau has lost its ability to enter the nucleus, which may result in DNA damage, due to the loss of the DNA-protective function of tau [80,105].”
BackgroundHSV-1 infection induces phosphorylated tau propagation among neurons via extracellular vesicles
Protto, V., Miteva, M. T., Iannuzzi, F., Marcocci, M. E., Puma, D. D. L., Piacentini, R., Belli, M., Sansone, L., Pietrantoni, A., Grassi, C., et al. (2024) · mBio · doi:10.1128/mbio.01522-24 · Cited by 26
“Specifically, some reports suggested that tau interaction with DNA could possibly either act as a transcript factor or alternatively protect DNA from external damage (37, 38).”
BackgroundTherapeutic and diagnostic challenges for frontotemporal dementia
Dâ€TMAlton, S., & Lewis, J. M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00204 · Cited by 26
“A nuclear form of tau is also implicated in protection from stress (Sultan et al., 2011), indicating that our current knowledge of tau function is probably incomplete.”
BackgroundCandia, R. F., Cohen, L. S., Morozova, V., Corbo, C. P., & Alonso, A. D. C. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.888420 · Cited by 24
The Involvement of Cholinergic Neurons in the Spreading of Tau Pathology
Simón, D., Hernández, F., & Avila, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00074 · Cited by 25
“A role in neuronal DNA protection has also been proposed (Sultan et al., 2011).”
BackgroundThe Cellular Distribution and Ser262 Phosphorylation of Tau Protein Are Regulated by BDNF In Vitro
Chen, Q., Zhou, Z., Zhang, L., Xu, S., Chen, C., & Yu, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091793 · Cited by 26
“increased tau expression may be a neuroprotective mechanism [40].”
BackgroundTau/DDX6 interaction increases microRNA activity
Chauderlier, A., Gilles, M., Špolcová, A., Caillierez, R., Chwastyniak, M., Kress, M., Drobecq, H., Bonnefoy, E., Pinet, F., Barbieri-Weill, D., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.06.006 · Cited by 26
Self-citationNoël, A., Barrier, L., & Ingrand, S. S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.06.020 · Cited by 24
Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23
Ng, P. Y., Chang, I. S., Koh, R. Y., & Chye, S. M. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00591-6 · Cited by 25
“Tau is mainly found in the somatodendritic compartment and axons but it also has been shown in dendrites and nucleus of neurons (Binder et al., 1985; Sultan et al. 2011; Hoover et al. 2010).”
BackgroundAshrafizadeh, M., Zarrabi, A., Najafi, M., Samarghandian, S., Mohammadinejad, R., & Ahn, K. S. (2020) · Phytotherapy Research · doi:10.1002/ptr.6732 · Cited by 24
Transcriptome analyses reveal tau isoform-driven changes in transposable element and gene expression
Grundman, J., Spencer, B., Sarsoza, F., & Rissman, R. A. (2021) · PLOS ONE · doi:10.1371/journal.pone.0251611 · Cited by 27
“Tau deficiency has been previously linked to DNA damage, and overexpression of tau in tau-deficient models has been shown to decrease DNA damage [10, 11].”
BackgroundMechanisms Underlying Aluminum Neurotoxicity Related to 14-3-3ζ Protein
Wang, X., Cheng, D., Jiang, W., & Ma, Y. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy021 · Cited by 23
Dangerous Liaisons: Tau Interaction with Muscarinic Receptors
Wysocka, A., Pałasz, E., Steczkowska, M., & Niewiadomska, G. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200424134311 · Cited by 24
Prion-like strain effects in tauopathies
Han, Z. Z., Kang, S., Arce, L., & Westaway, D. A. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03620-1 · Cited by 24
“2021), nucleic acid protection (Sultan et al. 2011; Violet et al. 2014), synaptic plasticity (Spires-Jones and Hyman 2014), and neuronal maturation (Fiock et al.”
BackgroundSauna-like conditions or menthol treatment reduce tau phosphorylation through mild hyperthermia
Guisle, I., Canet, G., Petry, S., Fereydouni-Forouzandeh, P., Morin, F., Kérauden, R., Whittington, R. A., Calon, F., Hébert, S. S., & Planel, E. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.02.011 · Cited by 23
Tau Protein as Therapeutic Target for Cancer? Focus on Glioblastoma
Hedna, R., Kovacic, H., Pagano, A., Peyrot, V., Robin, M., Devred, F., & Breuzard, G. (2022) · Cancers · doi:10.3390/cancers14215386 · Cited by 25
Heparan Sulfate Proteoglycans in Tauopathy
Zhu, Y., Gandy, L. A., Zhang, F., Liu, J., Wang, C., Blair, L. J., Linhardt, R. J., & Wang, L. (2022) · Biomolecules · doi:10.3390/biom12121792 · Cited by 27
Untangling the Role of Tau in Huntington’s Disease Pathology
Salem, S., & Cicchetti, F. (2023) · Journal of Huntington s Disease · doi:10.3233/jhd-220557 · Cited by 23
Rodríguez-Callejas, J. D., Fuchs, E., & Perez‐Cruz, C. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.04.010 · Cited by 23
Mutations in MAPT give rise to aneuploidy in animal models of tauopathy
Rossi, G., Conconi, D., Panzeri, E., Paoletta, L., Piccoli, E., Ferretti, M. G., Mangieri, M., Ruggerone, M., Dalprà, L., & Tagliavini, F. (2013) · Neurogenetics · doi:10.1007/s10048-013-0380-y · Cited by 23
“Evidence of both cytoplasmic and nuclear tau was given some years ago in neuroblastoma cell lines [20, 21] and very recently in primary cultures of mouse neurons [7, 15].”
BackgroundMaina, M. B., Al‐Hilaly, Y. K., Oakley, S. S., Burra, G., Khanom, T., Biasetti, L., Mengham, K., Marshall, K. E., Rickard, J. E., Harrington, C. R., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167785 · Cited by 23
Mumtaz, I., Ayaz, M. O., Khan, M. S., Manzoor, U., Ganayee, M. A., Bhat, A. Q., Dar, G. H., Alghamdi, B. S. A., Hashem, A. M., Dar, M. J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.977411 · Cited by 23
“Growing evidences report that dephosphorylated tau protects nuclear DNA from heat damage and other kinds of oxidative stress insults however tau in hyperphosphorylated form is believed to halt protective functionalities associated with non-phosphorylated forms in neuronal entities (Sultan et al., 2011).”
BackgroundShoeibi, A., Olfati, N., & Litvan, I. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1460356 · Cited by 23
“Physiologically, tau assembles and stabilizes microtubules (MT) and probably maintains integrity of nuclear DNA, mainly in the central nervous system [23,24].”
BackgroundDávila-Bouziguet, E., Fabra, G. T., Ávila, J., Soriano, E., & Pascual, M. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.12.006 · Cited by 23
Role of WWOX WOX1 in Alzheimer s disease pathology and in cell death signaling
Teng, C.-C. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s358 · Cited by 22
Biomarkers of mature neuronal differentiation and related diseases
Yuan, X., Li, W., Qi, Y., Ou, Y., Long, Q., & Zhang, P. (2024) · Future Science OA · doi:10.1080/20565623.2024.2410146 · Cited by 24
“Tau protein can directly bind to DNA and RNA, protecting them fr om oxidativ e damage and helping to maintain DNA and RNA int eg rity [ 50 ].”
BackgroundNon-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction
Siano, G., Falcicchia, C., Origlia, N., Cattaneo, A., & Primio, C. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810145 · Cited by 22
“This evidence suggests a protective role for Tau in the non-phosphorylated form that is supported by observations in mouse models where non-phosphorylated Tau levels are increased in neuronal nuclei after oxidative stress and hyperthermic conditions [115,118].”
BackgroundInoue, H., Hiradate, Y., Shirakata, Y., Kanai, K., Kosaka, K., Gotoh, A., Fukuda, Y., Nakai, Y., Uchida, T., Sato, E., et al. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.021 · Cited by 21
“This result agrees with the previous report [38].”
BackgroundResultThe Fast-Halo Assay for the Detection of DNA Damage
Sestili, P., Calcabrini, C., Diaz, A. R., Fimognari, C., & Stocchi, V. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7187-9_6 · Cited by 19
Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98
Diez, L., Kapinos, L. E., Hochmair, J., Hübschmann, S., Dominguez‐Baquero, A., Vogt, A., Rankovic, M., Zweckstetter, M., Lim, R. Y. H., & Wegmann, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073495 · Cited by 20
“Tau phosphorylation and redistribution into the somatodendritic compartment and into the nucleus occur upon neuronal stress exposure [6,7] and are seen as early changes related to Tau neurotoxicity in AD [8–10].”
BackgroundEvidence that Alzheimer’s Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry
Huang, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240042 · Cited by 20
Papegaey, A., Eddarkaoui, S., Deramecourt, V., Fernández-Gómez, F.-J., Pantano, P., Obriot, H., Machala, C., Anquetil, V., Camuzat, A., Brice, A., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0345-0 · Cited by 24
“However, recent studies have highlighted a role for Tau in synaptic [52, 53] and nuclear compartments [54, 55].”
BackgroundSelf-citationPhosphorylated nucleolar Tau protein is related to the neuronal in vitro differentiation
Federico, C., Gil, L., Bruno, F., D’Amico, A. G., D’Agata, V., & Saccone, S. (2018) · Gene · doi:10.1016/j.gene.2018.04.051 · Cited by 19
Wu, Z., Liu, X., Cheng, L., & Ye, K. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03270-7 · Cited by 18
Lozupone, M., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Altamura, M., Bellomo, A., et al. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2200245 · Cited by 21
“However, for ASO therapies, given the physiological functions of tau protein including synaptic plasticity [52], signaling [53] and nucleic acid protection [54,55], is mandatory a”
BackgroundTau: More than a microtubule‐binding protein in neurons
Alonso, A. D. C., Idrissi, A. E., Candia, R. F., Morozova, V., & Kleiman, F. E. (2023) · Cytoskeleton · doi:10.1002/cm.21795 · Cited by 17
“Oxidative and heat stresses trigger the accumulation of dephosphorylated tau in the nucleus, as well as promote the formation of tau-DNA complexes (Sultan et al., 2011).”
BackgroundFlores-Rodríguez, P., Harrington, C. R., Wischik, C. M., Ibarra-Bracamontes, V., Zarco, N., Navarrete, A., Martínez-Maldonado, A., Guadarrama-Ortíz, P., Villanueva‐Fierro, I., Ontiveros‐Torres, M. Á., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190155 · Cited by 18
“However, other investigators 612 have proposed mechanisms for tau protecting DNA 613 in heat-stressed neurons [55].”
Ke, Y. D., Dramiga, J., Schütz, U., Kril, J. J., Ittner, L. M., Schröder, H., & Götz, J. (2012) · PLoS ONE · doi:10.1371/annotation/6650167a-7567-4c65-931f-4be7145a39fc · Cited by 18
Tau protein binds to the P53 E3 ubiquitin ligase MDM2
Sola, M., Rendon-Angel, A., Martinez, V. R., Sgrignani, J., Magrin, C., Piovesana, E., Cavalli, A., Paganetti, P., & Papin, S. (2023) · Scientific Reports · doi:10.1038/s41598-023-37046-8 · Cited by 17
Sexton, C. E., Bitan, G., Bowles, K. R., Bryś, M., Buée, L., Maina, M. B., Clelland, C. D., Cohen, A. D., Crary, J. F., Dage, J. L., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13533 · Cited by 16
Self-citationPhospho-Tau and Chromatin Landscapes in Early and Late Alzheimer’s Disease
Gil, L., Niño, S. A., Guerrero, C., & Jiménez-Capdeville, M. E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910283 · Cited by 16
“The presence of tau in the nucleus, and especially in the nucleolus, has been widely reported [52,118,125,139].”
BackgroundRecent studies of atomic‐resolution structures of tau protein and structure‐based inhibitors
Zhu, L., & Qian, Z. (2021) · Quantitative Biology · doi:10.15302/j-qb-021-0271 · Cited by 16
Implications of Tau Dysregulation in Huntington’s Disease and Potential for New Therapeutics
Mees, I., Nisbet, R. M., Hannan, A. J., & Renoir, T. (2023) · Journal of Huntington s Disease · doi:10.3233/jhd-230569 · Cited by 16
“In addition to its microtubule-stabilizing functions, tau is thought to protect neuronal DNA [1] and regulate neurogenesis [2], neuronal activity [3], and long-term depression [4].”
BackgroundKoychev, I. G., Adler, A., Edison, P., Tom, B. D. M., Milton, J. E., Butchart, J., Hampshire, A., Marshall, C. R., Coulthard, E. J., Zetterberg, H., et al. (2024) · BMJ Open · doi:10.1136/bmjopen-2023-081401 · Cited by 16
“15 These results add to the growing appreciation that tau’s physiological role is significantly broader than neuronal structure support and includes regulation of insulin signalling, in addition to DNA protection from oxidative stress 16 and control of neuronal excitability.”
BackgroundPresynaptic Pathophysiology Encoded in Different Domains of Tau – Hyper-Versus Hypoexcitability?
Decker, J. M., & Mandelkow, E. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_8 · Cited by 15
Loss of DEK Expression Induces Alzheimer’s Disease Phenotypes in Differentiated SH-SY5Y Cells
Greene, A. N., Parks, L. G., Solomon, M. B., & Vinnedge, L. M. P. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.594319 · Cited by 15
“, 2014), where it can preserve DNA integrity in neurons (Sultan et al., 2011; Violet et al., 2014; Bukar Maina et al., 2016).”
BackgroundGlaucoma as a Tauopathy—Is It the Missing Piece in the Glaucoma Puzzle?
Passaro, M. L., Matarazzo, F., Abbadessa, G., Pezone, A., Porcellini, A., Tranfa, F., Rinaldi, M., & Costagliola, C. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12216900 · Cited by 16
“Tau is hypophosphorylated in the nucleus of neurons [127], and in vitro research has demonstrated that tau binds to the minor grooves of DNA to shield it from ROS [128].”
BackgroundTau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS
Kanaan, N. M. (2024) · Cytoskeleton · doi:10.1002/cm.21820 · Cited by 15
Tau Protein Alterations Induced by Hypobaric Hypoxia Exposure
Pena, E., Martin-Salamanca, R. S., Alam, S. E., Flores, K., & Arriaza, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020889 · Cited by 16
“In CNS neurons, the predominant MAP is tau, or microtubule-associated protein tau (MAPT), which is involved mainly in microtubule assembly and is mostly concentrated in neuronal axons [6,8,22,49,50].”
BackgroundRoqanian, S., Ahmadian, S., Nabavi, S. M., Pakdaman, H., Shafiezadeh, M., Goudarzi, G., & Shahpasand, K. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25024 · Cited by 15
Hu, Z., Jin, H., Xu, L., Zhu, Z., Jiang, Y., & Seal, R. L. (2013) · Pediatric Anesthesia · doi:10.1111/pan.12263 · Cited by 15
Phosphorylation of SET mediates apoptosis via P53 hyperactivation and NM23-H1 nuclear import
Wu, M., Yu, G., Yan, T., Ke, D., Wang, Q., Liu, R., Wang, J., Zhang, B., Chen, D., & Wang, X. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.04.022 · Cited by 14
Emerging Connections Between Tau and Nucleic Acids
Galas, M., Bonnefoy, E., Buée, L., & Lefebvre, B. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_12 · Cited by 17
Self-citationCimini, S., Giaccone, G., Tagliavini, F., Costantino, M., Perego, P., & Rossi, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115043 · Cited by 13
Regulating Phase Transition in Neurodegenerative Diseases by Nuclear Import Receptors
Girdhar, A., & Guo, L. E. (2022) · Biology · doi:10.3390/biology11071009 · Cited by 15
Tau oligomers accumulation sensitizes prostate cancer cells to docetaxel treatment
Martellucci, S., Clementi, L., Sabetta, S., Muzi, P., Mattei, V., Bologna, M., & Angelucci, A. (2021) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-021-03598-3 · Cited by 15
“More than a structural protein, tau is considered a guardian of DNA, playing a role during cellular stress, when it was shown to translocate to the nucleus, preventing stress-induced DNA breaks (Sultan et al. 2011).”
BackgroundJiang, Y., Zhou, Y. X., Tan, S., Xu, C., & Ma, J. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1113345 · Cited by 11
“, 2008), and perform functions at the dendrites in neurons (Ittner et al., 2010; Sultan et al., 2011).”
BackgroundExperimental Cell Models for Investigating Neurodegenerative Diseases
Evangelisti, C., Ramadan, S., Orlacchio, A., & Panza, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179747 · Cited by 16
“…and colleagues [26] suggested that the phosphorylation state and accumulation levels in subcellular compartments of Tau are modified by oxidative stress through mechanisms, which despite not being completely understood, have been observed previously in neuronal models of tauopathies [27].”
BackgroundSyntaxins 6 and 8 facilitate tau into secretory pathways
Lee, W. S., Tan, D. C. S., Deng, Y., van Hummel, A., Ippati, S., Stevens, C. H., Carmona-Mora, P., Ariawan, D., Hou, L., Stefen, H., et al. (2021) · Biochemical Journal · doi:10.1042/bcj20200664 · Cited by 13
Our Working Point of View of Tau Protein
Ávila, J. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170600 · Cited by 14
“cell nucleus [14, 15], where it can bind to nucleic acids [16, 17], and at the membrane [18, 19] has also been reported.”
BackgroundKhan, R. I., Nirzhor, S. S. R., & Rashid, B. (2018) · Brain Sciences · doi:10.3390/brainsci8090162 · Cited by 12
“In addition to axons and dendrites, nuclear tau are involved in the regulation of transcriptional activity and DNA/RNA maintenance under various physiological conditions [10,11,20,21].”
BackgroundFacile Installation of Post-translational Modifications on the Tau Protein via Chemical Mutagenesis
Lindstedt, P. R., Taylor, R. J., Bernardes, G. J. L., & Vendruscolo, M. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00761 · Cited by 12
“5 In addition, further vital functions are coming to light, such as the regulation of axonal transport, 6 DNA maintenance, 7 and regulation of synaptic function and plasticity.”
BackgroundUnknown roles of tau pathology in neurological disorders. Challenges and new perspectives
Olesen, M. A., Villavicencio-Tejo, F., Cuevas-Espinoza, V., & Quintanilla, R. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102594 · Cited by 12
Molecular Insights into Tau Pathology and its Therapeutic Strategies in Alzheimer's Disease
Zhou, F., Zhao, Y., Sun, Y., & Chen, W. (2024) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2311197 · Cited by 13
“Within neurons, nuclear tau exists mostly in a non-phosphorylated state during cellular stress [ 22].”
Ortiz-Islas, E., Montes, P., Rodríguez-Pérez, C. E., Ruiz-Sánchez, E., Sánchez-Barbosa, T., Pichardo-Rojas, D., Zavala‐Tecuapetla, C., Carvajal, K., & Campos‐Peña, V. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17010128 · Cited by 14
“Under oxidative or hyper-thermic stress conditions, the accumulation of dephosphorylated Tau in the nucleus of neurons is induced and necessary to protect DNA [109].”
Ketamine induces tau hyperphosphorylation at serine 404 in the hippocampus of neonatal rats.
Jin, H., Hu, Z., Dong, M., Wu, Y., Zhu, Z., & Xu, L. (2013) · PubMed Central · doi:10.3969/j.issn.1673-5374.2013.17.007 · Cited by 12
“They play an important role in the assembly of microtubules, contributing to axonal integrity of the normal mature neuron, but also playing a role at the dendritic and nuclear levels [7] .”
BackgroundWang, T., Yang, X., Qi, Z., Wang, G.-X., Xia, P., Hou, T., & Zhou, H. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.177744 · Cited by 12
“, 2015) and protection of neuronal DNA against oxygen free radicals (Sultan et al., 2011).”
BackgroundChauderlier, A., Delattre, L., Buée, L., & Galas, M. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_25 · Cited by 12
“This method offers the advantage of being noncytotoxic [7, 9] and easily useable with any kind of mouse, wild-type or transgenic.”
MethodSelf-citationCancer Cells Upregulate Tau to Gain Resistance to DNA Damaging Agents
Rico, T., Denéchaud, M., Caillierez, R., Comptdaer, T., Adriaenssens, É., Buée, L., & Lefebvre, B. (2022) · Cancers · doi:10.3390/cancers15010116 · Cited by 10
“In particular, an increase in γ-H2AX foci was observed under stress conditions in primary neuronal cell cultures in the absence of Tau or in the cortex and hippocampus of knock-out Tau mice [31,32].”
BackgroundSelf-citationCanet, G., Rocaboy, E., Laliberté, F., Boscher, E., Guisle, I., Diego-Diàz, S., Fereydouni-Forouzandeh, P., Whittington, R. A., Hébert, S. S., Pernet, V., et al. (2023) · Experimental Neurobiology · doi:10.5607/en23025 · Cited by 12
“Conversely, exposure to heat or thermogenesis-inducing drugs leads to tau dephosphorylation [12, 13].”
BackgroundGenomic stress and impaired DNA repair in Alzheimer disease
Neven, J., Issayama, L. K., Dewachter, I., & Wilson, D. M. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103678 · Cited by 12
Retinal tau phosphorylation in Alzheimer's disease: A mass spectrometry study
Santiago, J., Pocevičiūtė, D., Vogel, J. W., Bank, T. N. B., Brinkmalm, G., & Wennström, M. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107057 · Cited by 10
Danis, C., Dupré, E., Hanoulle, X., Landrieu, I., Lasorsa, A., Neves, J. F., Schneider, R., & Smet‐Nocca, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_3 · Cited by 12
Huda, M. N., Erdene-Ochir, E., & Pan, C. (2017) · Journal of Visualized Experiments · doi:10.3791/55932 · Cited by 11
Re-Arranging the Puzzle between the Amyloid-Beta and Tau Pathology: An APP-Centric Approach
Haut, F., Argyrousi, E. K., & Arancio, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010259 · Cited by 11
“Finally, in the nucleus, Tau maintains the integrity of genomic DNA as well as cytoplasmic and nuclear RNA [117,119].”
BackgroundChronic Formaldehyde-Mediated Impairments and Age-Related Dementia
Jun-Ye, M. I. A. O., & He, R. (2012) · InTech eBooks · doi:10.5772/34949 · Cited by 10
Fan, X., Truong, J. B., Okada, K., Lin, H., Ori-McKenney, K. M., & McKenney, R. J. (2026) · Communications Biology · doi:10.1038/s42003-026-10797-6 · Cited by 10
Ré, R. N. (2013) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e3182a28af3 · Cited by 9
The Implication of Glial Metabotropic Glutamate Receptors in Alzheimer’s Disease
de Lima, I. B. Q., & Ribeiro, F. M. (2021) · Current Neuropharmacology · doi:10.2174/1570159x20666211223140303 · Cited by 9
“Among the numerous tau post-translational modifications, phosphorylation is the most studied, having a central role in the regulation of tau function and cellular localization [59-62].”
Can accelerated ageing models inform us on age‐related tauopathies?
Han, Z. Z., Fleet, A., & Larrieu, D. (2023) · Aging Cell · doi:10.1111/acel.13830 · Cited by 10
Yu, Q., Li, L., Yu, S., Han, J., Cheng, Q., Cui, Z., Chen, H., Li, M., & Lu, Z. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04490-z · Cited by 9
“Beyond structural support, tau dynamically regulates microtubule assembly/disassembly through phosphorylation-dependent mechanisms, enabling neuronal plasticity and adaptive responses to synaptic activity [6].”
Atomic Force Microscopy Applied to the Study of Tauopathies
Amorim, M. D. S. D. N., França, Á. R. S., Santos‐Oliveira, R., Sanches, J. R., Melo, T. M., Pinto, B., Barbosa, L. R. S., & Alencar, L. M. R. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00819 · Cited by 7
Kanaan, N. M., Himmelstein, D. S., Ward, S., Combs, B., & Binder, L. I. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00056-1 · Cited by 9
Gratuze, M., Joly‐Amado, A., Buée, L., Vieau, D., & Blum, D. L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_21 · Cited by 8
Self-citationLooking at Alzheimer’s Disease Pathogenesis from the Nuclear Side
D’Andrea, L., Stringhi, R., Luca, M. D., & Marcello, E. E. (2021) · Biomolecules · doi:10.3390/biom11091261 · Cited by 8
Oligomeropathies, inflammation and prion protein binding
Forloni, G., Vitola, P. L., & Balducci, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.822420 · Cited by 8
“In the cell nuclei tau exerts neuroprotective activity, interacting with DNA regions of the chromosome (Sjöberg et al., 2006; Sultan et al., 2011), so tau oligomerization may cause a loss of physiological function (Benhelli-Mokrani et al.”
BackgroundAging-associated REGγ proteasome decline predisposes to tauopathy
Tu, J., Zhang, H., Yang, T., Liu, Y., Kibreab, S., Zhang, Y., Gao, L., Moses, R. E., O’Malley, B. W., Xiao, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102571 · Cited by 9
“The cDNA was subjected to qRT-PCR using ChamQ SYBR qPCR Master Mix (High ROX Premixed) (Vazyme) and Quant Studio 3.0 (Thermo Scientific).”
BackgroundInfluentialApolipoprotéine E et intégrité de la barrière hémato-encéphalique
Gosselet, F. (2012) · médecine/sciences · doi:10.1051/medsci/20122811006 · Cited by 8
“Des études tout génome (GWAS), menées sur différentes populations, ont actuellement identifié trois sites régulateurs dont la somme n’explique, cependant, qu’environ 50 % des variations observées [1].”
BackgroundLu, S., Qiu, S., Yu, G., Zhang, A., & Zhao, Q. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103097 · Cited by 8
The emerging complexity of molecular pathways implicated in mouse self-grooming behavior
Ikrin, A. N., Moskalenko, A. M., Mukhamadeev, R. R., de Abreu, M. S., Kolesnikova, T. O., & Kalueff, A. V. (2023) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2023.110840 · Cited by 7
Tau beyond Tangles: DNA Damage Response and Cytoskeletal Protein Crosstalk on Neurodegeneration
Asada‐Utsugi, M., & Urushitani, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147906 · Cited by 8
“Tau may be associated with DDR because of its DNA-binding capacity and reports on chromatin remodeling [48,49].”
BackgroundÁvila, J., Gómez‐Ramos, A., & Soriano, E. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00323 · Cited by 7
“Tau protein is not only a cytoskeletal protein but it is found in the nucleus of neurons (Wang et al., 1993; Brady et al., 1995; Lambert et al., 1995; Sultan et al., 2011).”
BackgroundTang, X., Jiao, L., Zheng, M., Yan, Y., Nie, Q., Wu, T., Wan, X., Zhang, G., Li, Y., Wu, S., et al. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.01.002 · Cited by 7
“…to be involved in multiple novel functions, including long-term depression (LTD), chromosome stability and DNA protection, adult neurogenesis as well as modulation of enzymatic activity (Perez et al., 2009; Hong et al., 2010; Sultan et al., 2011; Kimura et al., 2014; Wang and Mandelkow, 2016).”
BackgroundEGCG modulates nuclear formaldehyde-induced Tau phosphorylation in Neuronal cellsPreprint
Sonawane, S. K., Raina, A., Majumdar, A., & Chinnathambi, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.04.325134 · Cited by 7
Juarez-Romero, G. U., Sun, X., Gerez, J., Auwer, C. D., Landrot, G., Nachtegaal, M., Riek, R., Luo, J., & Quintanar, L. (2026) · Chemical Science · doi:10.1039/d5sc08604c · Cited by 7
“93,94 The nucleus is a zinc-rich cellular compartment; 95 hence, the Zn binding site 1 in tau could be populated, potentially modulating its interaction with DNA.”
Gazarian, K. G., Ramírez-García, L. R., Orozco, L. T., Luna‐Muñoz, J., & Pacheco‐Herrero, M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.612657 · Cited by 6
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
