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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]
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“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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Hanger, D. P., Lau, D. H. W., Phillips, E. C., Bondulich, M. K., Guo, T., Woodward, B. W., Pooler, A. M., & Noble, W. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132054 · Cited by 66
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“This interaction with DNA indicates that tau proteins may play a role in protection against reactive oxygen species (36, 37), ribosome stability and miRNA activity (38).”
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“, 2011) and in the nucleus (Sultan et al., 2011; Mansuroglu et al., 2016) regulating cell signaling, genome expression and stability, and neuronal plasticity at synapses.”
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“In this respect, a role of tau in neuronal DNA protection has been recently described (Sultan et al., 2011).”
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Fontaine, S. N., Sabbagh, J. J., Baker, J. D., Licha, C. R. M., Darling, A. L., & Dickey, C. A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1839-9 · Cited by 66
“Tau can also be found localized in the nucleus [112], bound to AT-rich polynucleotide sequences and has been reported to protect DNA from stress-induced damage [113] and function in nucleolar organization [114].”
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Xu, Y., Uronen, R., & Huttunen, H. J. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.05.005 · Cited by 64
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Rossi, G., & Tagliavini, F. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00192 · Cited by 62
“Pathologically, deposits of different misfolded proteins are found in brain tissue: tau, transactive response DNA binding protein 43, fused-in-sarcoma, and dipeptide-repeat proteins.”
BackgroundInfluentialFerrari, R., Forabosco, P., Vandrovcová, J., Botía, J. A., Guelfi, S., Warren, J. D., Momeni, P., Weale, M. E., Ryten, M., & Hardy, J. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0085-4 · Cited by 57
“involvement in DNA binding and given evidence for its involvement in DNA protection [35], it follows that tau”
BackgroundSchirer, Y., Malishkevich, A., Ophir, Y., Lewis, J. M., Giladi, E., & Gozes, I. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087383 · Cited by 57
“providing protection against DNA damage [19], while ectopic”
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Merezhko, M., Uronen, R., & Huttunen, H. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569818 · Cited by 65
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“Previous research from our group as well as others, working in the field of tauopathies, has shown (i) a nuclear distribution for Tau protein in neuronal and non-neuronal cells (11,17,18), (ii) that Tau protein binds nucleic acids and forms protein-DNA complexes (11,19–21), (iii) that gene expression deregulation acco…”
BackgroundMethodResultInfluentialSelf-citationPhosphorylation of nuclear Tau is modulated by distinct cellular pathways
Ulrich, G., Salvadè, A., Boersema, P. J., Calí, T., Foglieni, C., Sola, M., Picotti, P., Papin, S., & Paganetti, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-36374-4 · Cited by 52
From epidemiology to pathophysiology: what about caffeine in Alzheimer's disease?
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Self-citationHippocampal GFAP-positive astrocyte responses to amyloid and tau pathologies
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N-terminal Truncation of Microtubule Associated Protein Tau Dysregulates its Cellular Localization
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“ous observations [3] and in a good correlation with”
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Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin
Abasi, L. S., Elathram, N., Movva, M., Deep, A., Corbett, K. D., & Debelouchina, G. T. (2024) · Communications Biology · doi:10.1038/s42003-024-05920-4 · Cited by 55
“Stress conditions such as heat shock and oxidative stress induceanincreasedtranslocationoftauintothenucleus,whichisassociated withaDNA-protectiveeffect,whiletaudepletionisassociatedwithgenomic instability 29,30,32 .”
Emerging Evidences for an Implication of the Neurodegeneration-Associated Protein TAU in Cancer
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“In particular, several groups have observed that TAU may participate in modifying genomic stability [51], DNA protection [73,74], and heterochromatin state [75], key processes deregulated in cancer.”
BackgroundTau Spreading Mechanisms; Implications for Dysfunctional Tauopathies
Fuster-Matanzo, A., Hernández, F., & Ávila, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030645 · Cited by 50
“Additionally, in the nucleus of neurons and non-neuronal cells, tau is believed to be key in maintaining the integrity of genomic DNA, cytoplasmic RNA and nuclear RNA [22,29].”
BackgroundDNA repair deficiency and senescence in concussed professional athletes involved in contact sports
Schwab, N., Grenier, K., & Hazrati, L.-N. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0822-3 · Cited by 47
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Špolcová, A., Mikulášková, B., Holubová, M., Pražienková, V., Pirník, Z., Zemenová, J., Haluzı́k, M., Železná, B., Galas, M., & Maletı́nská, L. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-143150 · Cited by 47
“identified previously [32] and anti- -actin antibody produced in mouse were obtained from Sigma-Aldrich, St.”
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Neuronal nuclear tau and neurodegeneration
Antón‐Fernández, A., Vallés‐Saiz, L., Ávila, J., & Hernández, F. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.015 · Cited by 45
“This suggested the potential interaction of tau with protein chromatin components besides its interaction with DNA (Sultan et al., 2011).”
BackgroundGlobal Analysis of Phosphorylation of Tau by the Checkpoint Kinases Chk1 and Chk2 in vitro
Mendoza, J., Sekiya, M., Taniguchi, T., Iijima, K., Wang, R., & Ando, K. (2013) · Journal of Proteome Research · doi:10.1021/pr400008f · Cited by 45
Mutual Relationship between Tau and Central Insulin Signalling: Consequences for AD and Tauopathies?
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Developmental Expression of 4-Repeat-Tau Induces Neuronal Aneuploidy in Drosophila Tauopathy Models
Malmanche, N., Dourlen, P., Gistelinck, M., Demiautte, F., Link, N., Dupont, C., Broeck, L. V., Werkmeister, E., Amouyel, P., Bongiovanni, A., et al. (2017) · Scientific Reports · doi:10.1038/srep40764 · Cited by 48
“1038/srep40764 almost normal mitotic timing (15 to 20 minutes) and a normal anaphase progression (Sup Movie S3 arrowhead), (3) cells with a mitotic timing ranging from more than 20 minutes up to 35 minutes and for which chromosome hypercondensation and spindle collapse are visible at metaphase Sup Movie S2 arrow), (4)…”
BackgroundThe prion-like transmission of tau oligomers via exosomes
Jackson, N. A., Guerrero‐Munoz, M. J., & Castillo‐Carranza, D. L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.974414 · Cited by 46
“The proline-rich domain of tau interacts with DNA (Sultan et al., 2011).”
BackgroundRecent developments with tau-based drug discovery
Iqbal, K., Liu, F., & Gong, C. (2018) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2018.1445084 · Cited by 46
McVicker, D. P., Hoeprich, G. J., Thompson, A. R., & Berger, C. L. (2014) · Cytoskeleton · doi:10.1002/cm.21163 · Cited by 40
“…ability to regulate microtubule spacing [Chen et al., 1992; Frappier et al., 1994], involvement in multiple signaling pathways [Perez et al., 2009; Sultan et al., 2011; Li et al., in press], and the regulation kinesin-mediated transport [Vershinin et al., 2007; Dixit et al., 2008; Stoothoff et…”
BackgroundVisualizing the microtubule-associated protein tau in the nucleus
Lu, J. N., Li, T., He, R., Bartlett, P. F., & Götz, J. (2014) · Science China Life Sciences · doi:10.1007/s11427-014-4635-0 · Cited by 43
Tau and DNA Damage in Neurodegeneration
Colnaghi, L., Rondelli, D., Muzi-Falconi, M., & Sertic, S. (2020) · Brain Sciences · doi:10.3390/brainsci10120946 · Cited by 42
“In the past decade, new and unexpected roles of tau have emerged in the nucleus and in the maintenance of genome stability [19,37].”
BackgroundResultInfluentialMelatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders
Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 45
Montalbano, M., Jaworski, E. A., García, S., Ellsworth, A., McAllen, S., Routh, A. L., & Kayed, R. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.742790 · Cited by 40
Structural studies on the mechanism of protein aggregation in age related neurodegenerative diseases
Eftekharzadeh, B., Hyman, B. T., & Wegmann, S. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.03.001 · Cited by 44
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“Although this protein is mainly found in the cytosol of neuronal cells, it has also been localized within the nucleus of both neuronal [13-19] and non-neuronal cells [20-23].”
InfluentialFurther understanding of tau phosphorylation: implications for therapy
Medina, M., & Avila, J. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1000864 · Cited by 41
“Such functions include neuronal polarization, axonogenesis, interactions with the plasma membrane and scaffold proteins, signal transduction, cell cycle, DNA protection or determination of dendritic spine density [24,27].”
BackgroundLessons from two prevalent amyloidoses—what amylin and Aβ have in common
Götz, J., Lim, Y.-A., & Eckert, A. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00038 · Cited by 40
Oxidative Stress Modifies the Levels and Phosphorylation State of Tau Protein in Human Fibroblasts
Ibáñez-Salazar, A., Bañuelos-Hernández, B., Rodríguez‐Leyva, I., Chi-Ahumada, É., Monreal‐Escalante, E., Jiménez-Capdeville, M. E., & Rosales‐Mendoza, S. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00495 · Cited by 43
“Audrey et al. (2011) observed in neuron culture assays, subjected to oxidative stress, an accumulation of dephosphorylated tau in the nuclei.”
BackgroundResultInfluentialNuclear Transport Deficits in Tau-Related Neurodegenerative Diseases
Diez, L., & Wegmann, S. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01056 · Cited by 40
“A pronounced accumulation of Tau-1 positive tau in the nucleus was observed upon acute oxidative and heat stress both in vitro and in vivo (52).”
BackgroundInfluentialGenome instability and loss of protein homeostasis: converging paths to neurodegeneration?
Ainslie, A. P., Huiting, W., Barazzuol, L., & Bergink, S. (2021) · Open Biology · doi:10.1098/rsob.200296 · Cited by 42
“By contrast, other studies have reported that nuclear Tau protects the DNA fromdamage in cell culture under stress conditions [67] (figure 2).”
ResultThermodynamics of the Interaction between Alzheimer's Disease Related Tau Protein and DNA
Camero, S., Benítez, M. J., Cuadros, R., Hernández, F., Ávila, J., & Jiménez, J. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104690 · Cited by 40
“The full process is reversed when the insult ceases [24].”
BackgroundInfluentialMari, S. A., Wegmann, S., Tepper, K., Hyman, B. T., Mandelkow, E., Mandelkow�, E., & Müller, D. J. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b01085 · Cited by 39
Distinct Conformations, Aggregation and Cellular Internalization of Different Tau Strains
Karikari, T. K., Nagel, D. A., Grainger, A. I., Clarke-Bland, C., Crowe, J. A., Hill, E. J., & Moffat, K. G. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00296 · Cited by 41
Somatic Signature of Brain-Specific Single Nucleotide Variations in Sporadic Alzheimer's Disease
Parcerisas, A., Rubio, S. E., Muhaisen, A., Gómez-Ramos, A., Pujadas, L., Puiggros, M., Rossi, D., Ureña, J., Burgaya, F., Pascual, M., et al. (2014) · Journal of Alzheimer’s Disease · doi:10.3233/jad-140891 · Cited by 44
The ‘a, b, c’s of pretangle tau and their relation to aging and the risk of Alzheimer’s Disease
Harley, C. W., Walling, S. G., Yuan, Q., & Martin, G. M. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.12.010 · Cited by 41
The propagation mechanisms of extracellular tau in Alzheimer’s disease
Wei, Y., Liu, M., & Wang, D. (2021) · Journal of Neurology · doi:10.1007/s00415-021-10573-y · Cited by 40
Tau Mutations Serve as a Novel Risk Factor for Cancer
Rossi, G., Redaelli, V., Contiero, P., Fabiano, S., Tagliabue, G., Perego, P., Benussi, L., Bruni, A. C., Filippini, G., Farinotti, M., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3175 · Cited by 38
“Additionally, a link between tau and genome integrity was evidenced when tau was shown to translocate from the cytoplasm to the nucleus during cellular stress and to protect DNA from stress-induced DNA breaks (19).”
BackgroundThe Involvement of Aβ42 and Tau in Nucleolar and Protein Synthesis Machinery Dysfunction
Maina, M. B., Bailey, L. J., Doherty, A. J., & Serpell, L. C. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00220 · Cited by 38
Implications of mRNA translation dysregulation for neurological disorders
Jishi, A., Qi, X., & Miranda, H. C. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.09.005 · Cited by 40
Main, H. G., Yu, Y., Choi, J. J., Kajdacsy‐Balla, A., & Barbolina, M. V. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16023419 · Cited by 37
O -GlcNAc cycling and the regulation of nucleocytoplasmic dynamics
Eustice, M., Bond, M. R., & Hanover, J. A. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160171 · Cited by 37
Neurodegenerative Disease-Related Proteins within the Epidermal Layer of the Human Skin
Åkerman, S., Hossain, S., Shobo, A., Zhong, Y., Jourdain, R., Hancock, M. A., George, K. M., Breton, L., & Multhaup, G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181191 · Cited by 35
“Recent studies have provided insight to the role of nuclear tau where it is suggested to be involved in DNA protection and repair in response to cellular stress [44, 45].”
What’s in a Gene? The Outstanding Diversity of MAPT
Ruiz-Gabarre, D., Carnero-Espejo, A., Ávila, J., & García‐Escudero, V. (2022) · Cells · doi:10.3390/cells11050840 · Cited by 39
“In line with its nuclear localisation, Tau protein has been demonstrated to bind to DNA in vitro [88,89] and in vivo [90] and RNA [91], as well as interact with chromatin components [92] and the inner side of the nuclear lamina [93].”
BackgroundTau truncation in the pathogenesis of Alzheimer’s disease: a narrative review
Chu, D., Yang, X., Wang, J., Zhou, Y., Gu, J., Miao, J., Wu, F., & Liu, F. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385853 · Cited by 39
“Under acute oxidative stress and mild heat stress conditions, more Tau proteins translocate into the nucleus, interacting with neuronal DNA and protecting the genomic DNA Review integrity from stress (Sultan et al., 2011).”
BackgroundTau Abnormalities and the Potential Therapy in Alzheimer’s Disease
Almansoub, H. A. M. M., Tang, H. R., Wu, Y., Wang, D., Mahaman, Y. A. R., Wei, N., Almansob, Y. A. M., He, W., & Liu, D. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180868 · Cited by 39
Tau, tau kinases, and tauopathies: An updated overview
Montalto, G., & Ricciarelli, R. (2023) · BioFactors · doi:10.1002/biof.1930 · Cited by 39
Alterations in Tau Metabolism in ALS and ALS-FTSD
Strong, M. J., Donison, N. S., & Volkening, K. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.598907 · Cited by 37
“A tau isoform that lacks phosphorylation at S195-S202 is localized to the nucleus, where it is involved in DNA binding (either through association with AT-rich DNA, or with the minor groove of AT-rich DNA sequences) (55, 56), heterochromatin stability, transcription repression of ribosomal DNA, long non-coding RNA pro…”
BackgroundHow it all Started: Tau and Protein Phosphatase 2A
Liu, C., & Götz, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130503 · Cited by 38
“nucleus in protecting DNA from damage such as heat shock or oxidative stress [80].”
BackgroundShaping of interphase chromosomes by the microtubule network
Maizels, Y., & Gerlitz, G. (2015) · FEBS Journal · doi:10.1111/febs.13334 · Cited by 33
Gil, L., Niño, S. A., Chi-Ahumada, É., Rodríguez‐Leyva, I., Guerrero, C., Poves, A. B. R., Navalón, J. A. A., & Jiménez-Capdeville, M. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051841 · Cited by 34
Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 39
“This more dynamic view of tau has diversified the repertoire of tau’s involvement in cellular processes to include increasing microtubule dynamics and the length of labile domains in microtubules [27], modulating axonal transport [28], regulating synaptic plasticity [29], maintaining genomic integrity [30,31], control…”
BackgroundCallari, M., Sola, M., Magrin, C., Rinaldi, A., Bolis, M., Paganetti, P., Colnaghi, L., & Papin, S. (2023) · Scientific Data · doi:10.1038/s41597-023-02543-y · Cited by 36
“For instance, DNA lesions accumulate in the brains of MAPT knock-out ( MAPT KO) mice or primary neurons 7,8 .”
Nuclear face of Tau: an inside player in neurodegeneration
Younas, N., Saleem, T., Younas, A., & Zerr, I. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01702-x · Cited by 34
“…Tau protein with DNA can increase the melting temperature of DNA [65] and protect it against heat shock induced double strand breaks, providing an evidence that nuclear Tau (non-phosphorylated) is crucial to cope with early stress responses in continuous changing microenvironment of neurons [66].”
BackgroundÁvila, J., Pallas‐Bazarra, N., Bolós, M., Sayas, C. L., & Hernández, F. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1131269 · Cited by 36
Prakash, A., Shin, J. S., Rajan, S. S., & Yoon, H. S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw001 · Cited by 31
“Several proteins, which are known to interact with DNA in a sequence-independent manner, were shown to be involved in DNA repair or have a role in chromatin re-modeling (17,46,56–58).”
Stevens, C. H., Guthrie, N. J., van Roijen, M., Halliday, G. M., & Ooi, L. (2019) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlz041 · Cited by 28
“A change in tau phosphorylation is suggested to be responsible for alterations in nuclear tau; however, the exact mechanism of entry into the nucleus is still not known (39).”
BackgroundFunctional significance of O-GlcNAc modification in regulating neuronal properties
Hwang, H., & Rhim, H. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.006 · Cited by 32
Bashir, S., Aiman, A., Shahid, M., Chaudhary, A. A., Sami, N., Basir, S. F., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102276 · Cited by 31
Daude, N., Kim, C., Kang, S., Eskandari‐Sedighi, G., Haldiman, T., Yang, J., Fleck, S. C., Gomez‐Cardona, E., Han, Z. Z., Borrego‐Écija, S., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02148-4 · Cited by 30
“6a) brings to mind reports of tau within the nucleus and in perturbations of the nuclear membrane and import/export processes [9, 15, 28, 73, 102].”
BackgroundGiong, H.-K., Subramanian, M., Yu, K., & Lee, J.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168465 · Cited by 31
“In addition, Tau is found in the nucleus, where it binds to the heterochromatin and protects the integrity of DNA and RNA [22,23], and is localized in the neural plasma membrane in a MT-independent manner [24,25].”
BackgroundDenéchaud, M., Geurs, S., Comptdaer, T., Bégard, S., García-Núñez, A., Pechereau, L.-A., Bouillet, T., Vermeiren, Y., Deyn, P. P. D., Perbet, R., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102386 · Cited by 29
Self-citationMilenković, I., Jarc, J., Dassler, E., Aronica, E., Iyer, A. M., Adle‐Biassette, H., Scharrer, A., Reischer, T., Hainfellner, J. A., & Kovács, G. G. (2017) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12406 · Cited by 29
Aging and Alzheimer’s disease connection: Nuclear Tau and lamin A
Gil, L., Niño, S. A., Capdeville, G., & Jiménez-Capdeville, M. E. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135741 · Cited by 31
Rane, J. S., Kumari, A. R., & Panda, D. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00455 · Cited by 27
Cellular Biology of Tau Diversity and Pathogenic Conformers
Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29
“, oxidative and mild heat stresses) (45, 46) and participates in RNA metabolism through direct association with RNA-binding proteins (47, 48).”
BackgroundMacromolecular Structures and Proteins Interacting with the Microtubule Associated Tau Protein
Jiménez, J. S. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.05.023 · Cited by 28
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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