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Tau pathology in Alzheimer disease and other tauopathies
Open accessAbstract
Just as neuronal activity is essential to normal brain function, microtubule-associated protein tau appears to be critical to normal neuronal activity in the mammalian brain, especially in the evolutionary most advanced species, the homo sapiens. While the loss of functional tau can be compensated by the other two neuronal microtubule-associated proteins, MAP1A/MAP1B and MAP2, it is the dysfunctional, i.e., the toxic tau, which forces an affected neuron in a long and losing battle resulting in a slow but progressive retrograde neurodegeneration. It is this pathology which is characteristic of Alzheimer disease (AD) and other tauopathies. To date, the most established and the most compelling cause of dysfunctional tau in AD and other tauopathies is the abnormal hyperphosphorylation of tau. The abnormal hyperphosphorylation not only results in the loss of tau function of promoting assembly and stabilizing microtubules but also in a gain of a toxic function whereby the pathological tau sequesters normal tau, MAP1A/MAP1B and MAP2, and causes inhibition and disruption of microtubules. This toxic gain of function of the pathological tau appears to be solely due to its abnormal hyperphosphorylation because dephosphorylation converts it functionally into a normal-like state. The affected neurons battle the toxic tau both by continually synthesizing new normal tau and as well as by packaging the abnormally hyperphosphorylated tau into inert polymers, i.e., neurofibrillary tangles of paired helical filaments, twisted ribbons and straight filaments. Slowly but progressively, the affected neurons undergo a retrograde degeneration. The hyperphosphorylation of tau results both from an imbalance between the activities of tau kinases and tau phosphatases and as well as changes in tau's conformation which affect its interaction with these enzymes. A decrease in the activity of protein phosphatase-2A (PP-2A) in AD brain and certain missense mutations seen in frontotemporal dementia promotes the abnormal hyperphosphorylation of tau. Inhibition of this tau abnormality is one of the most promising therapeutic approaches to AD and other tauopathies.
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“Among the several kinases involved in tau hyperphosphorylation (Singh et al., 1994;Johnson and Hartigan, 1999), CDK5 and GSK3 have been most implicated in the abnormal hyperphosphorylation of tau (Imahori and Uchida, 1997;Shelton and Johnson, 2004;Iqbal et al., 2005).”
From Retinoic Acid Attenuates β-Amyloid Deposition and Rescues Memory Deficits in an Alzheimer's Disease Transgenic Mouse Model (2008) · cites this paper as Iqbal et al., 2005
Citations
Cites
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES
Cohen, P. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.002321 · Cited by 2,543
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Observations on the brains of demented old people
Tomlinson, B. E., Blessed, G., & Roth, M. (1970) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(70)90063-8 · Cited by 2,084
Memantine in Moderate-to-Severe Alzheimer's Disease
Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
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Kowalska, M., Wize, K., Prendecki, M., Lianeri, M., Kozubski, W. P., & Dorszewska, J. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200224121447 · Cited by 34
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Dai, M., Freeman, B. D., Shikani, H. J., Bruno, F., Collado, J., Macias, R., Reznik, S. E., Davies, P. J., Spray, D. C., Tanowitz, H. B., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044117 · Cited by 32
Townsend, D. J., Fullwood, N. J., Yates, E. A., & Middleton, D. A. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00443 · Cited by 32
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Carreras, I., McKee, A. C., Choi, J., Aytan, N., Kowall, N. W., Jenkins, B. G., & Dedeoglu, A. (2013) · Brain Research · doi:10.1016/j.brainres.2013.10.025 · Cited by 35
Mendes, N. D., Fernandes, A., de Almeida, G. M., Santos, L. E., Sellés, M. C., Silva, N. M. L. E., Machado, C. D. M., Horta‐Júnior, J. D. A. C., Louzada, P. R., Felice, F. G. D., et al. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.05.021 · Cited by 35
Li, T., & Paudel, H. K. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2006.11.073 · Cited by 32
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Tzekaki, E. E., Papaspyropoulos, A., Tsolaki, M., Lazarou, E., Kozori, M., & Pantazaki, Α. A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111178 · Cited by 31
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Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32
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Rekha, A., Afzal, M., Babu, M. A., Menon, S. V., Nathiya, D., Supriya, S., Mishra, S. B., Gupta, S., Goyal, K., Rana, M., et al. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.104005 · Cited by 34
Falsetti, L., Viticchi, G., Zaccone, V., Guerrieri, E., Moroncini, G., Luzzi, S., & Silvestrini, M. (2022) · Biomedicines · doi:10.3390/biomedicines10020439 · Cited by 30
Chen, C., Hou, Y., Liu, J., Wu, Y., Lin, C., Fung, H., Hsu, W., Hsu, Y., Lee, S., Hsieh-Li, H.-M., et al. (2008) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30785 · Cited by 30
Connell‐Crowley, L., Vo, D. J., Luke, L., & Giniger, E. (2007) · Mechanisms of Development · doi:10.1016/j.mod.2007.02.002 · Cited by 30
Tissot, C., Servaes, S., Lussier, F. Z., Ferrari‐Souza, J. P., Therriault, J., Ferreira, P. C. L., Bezgin, G., Bellaver, B., Leffa, D. T., Mathotaarachchi, S. S., et al. (2022) · Journal of Nuclear Medicine · doi:10.2967/jnumed.122.264434 · Cited by 30
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
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Massalimova, A., Ni, R., Nitsch, R. M., Reisert, M., von Elverfeldt, D., & Klohs, J. (2020) · Neurodegenerative Diseases · doi:10.1159/000515754 · Cited by 28
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Koss, D. J., Hindley, K. P., Riedel, G., & Platt, B. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04579.x · Cited by 28
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Early postnatal lead exposure induces tau phosphorylation in the brain of young rats
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Ward, S. M., Himmelstein, D. S., Ren, Y., Fu, Y., Yu, X., Roberts, K. F., Binder, L. I., & Sahara, N. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.03.002 · Cited by 28
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Sazonova, M. A., Sinyov, V. V., Ryzhkova, A. I., Sazonova, M. D., Kirichenko, T. V., Khotina, V. A., Khasanova, Z. B., Doroschuk, N. A., Karagodin, V. P., Orekhov, A. N., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020699 · Cited by 27
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Ren, Q., Liao, X., Wang, X., Qu, Z.-S., & Wang, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.073 · Cited by 26
To be or not to be: the regulation of mRNA fate as a survival strategy during mammalian hibernation
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Tautvydaitė, D., Kukreja, D., Antonietti, J., Henry, H., von Gunten, A., & Popp, J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0235-0 · Cited by 28
Dhanabalan, A. K., Kesherwani, M., Velmurugan, D., & Gunasekaran, K. (2017) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2017.06.001 · Cited by 26
Hu, J., Yang, Y., Wang, M., Yao, Y., Chang, Y., He, Q., Ma, R., & Li, G. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.02.020 · Cited by 26
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Hu, X., Meier, M., & Pruessner, J. C. (2023) · Brain and Behavior · doi:10.1002/brb3.2925 · Cited by 24
Sharma, P., & Singh, M. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121568 · Cited by 25
Kellett, K. A. B., & Hooper, N. M. (2015) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-7197-9_17 · Cited by 25
Huang, A., & Stultz, C. M. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.40 · Cited by 26
Watamura, N., Toba, J., Yoshii, A., Nikkuni, M., & Ohshima, T. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23674 · Cited by 25
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Chang, K., Lin, C., Chen, H., Huang, H., Chen, S., Lin, T., Ramesh, C., Huang, C., Fung, H., Wu, Y., et al. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12592 · Cited by 25
Sandhu, P., Naeem, M. M., Lu, C., Kumarathasan, P., Gomes, J., & Basak, A. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.11.087 · Cited by 25
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Frenkel‐Pinter, M., Tal, S., Scherzer‐Attali, R., Abu-Hussien, M., Alyagor, I., Eisenbaum, T., Gazit, E., & Segal, D. (2016) · Neurodegenerative Diseases · doi:10.1159/000448518 · Cited by 24
Calabrese, V. (2017) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2017/2.942x/2017/1.1088 · Cited by 24
Delbreil, P., Rabanel, J., Banquy, X., & Brambilla, D. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114397 · Cited by 25
Cyclic dipeptide‐based small molecules modulate zinc‐mediated liquid–liquid phase separation of tau
Ramesh, M., Balachandra, C., Baruah, P., & Govindaraju, T. (2022) · Journal of Peptide Science · doi:10.1002/psc.3465 · Cited by 25
Hallows, J. L., Iosif, R. E., Biasell, R. D., & Vincent, I. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4834-05.2006 · Cited by 24
Mendonca, P., Taka, E., Bauer, D. F., Cobourne-Duval, M. K., & Soliman, K. (2017) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2017.01.011 · Cited by 25
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Sedjahtera, A., Gunawan, L., Bray, L., Hung, L. W., Parsons, J., Okamura, N., Villemagne, V. L., Yanai, K., Liu, X. M., Chan, J., et al. (2018) · Metallomics · doi:10.1039/c8mt00153g · Cited by 24
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Liu, H., Jin, X., Yin, X., Jin, N., Liu, F., & Qian, W. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142610 · Cited by 25
Blard, O., Frébourg, T., Campion, D., & Lecourtois, M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21006 · Cited by 24
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Dalby, N. O., Volbracht, C., Helboe, L., Larsen, P. H., Jensen, H. S., Egebjerg, J., & Elvang, A. B. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131358 · Cited by 23
Pan, B., Lu, X., Han, X., Huan, J., Gao, D., Cui, S., Ju, X., Zhang, Y., Xu, S., Song, J., et al. (2021) · ACS Omega · doi:10.1021/acsomega.1c04434 · Cited by 23
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Li, J., Kumar, A., Långström, B., Nordberg, A. K., & Ågren, H. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00437 · Cited by 25
Cerebrospinal fluid biomarkers of Alzheimer’s disease in cognitively healthy elderly
Glodzik, L. (2013) · Frontiers in bioscience · doi:10.2741/4170 · Cited by 25
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Yotsumoto, K., Saito, T., Asada, A., Oikawa, T., Kimura, T., Uchida, C., Ishiguro, K., Uchida, T., Hasegawa, M., & Hisanaga, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003277 · Cited by 23
Rossi, F., Geiszler, P. C., Meng, W., Barron, M. R., Prior, M. J. W., Herd-Smith, A., Loreto, A., Lopez, M. Y., Faas, H., Pardon, M., et al. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.11.030 · Cited by 24
Gandy, J. C., Meléndez‐Ferro, M., Bijur, G. N., LEUVEN, F. V., Roche, J. K., Lechat, B., Devijver, H., Demedts, D., Pérez‐Costas, E., & Roberts, R. C. (2013) · Synapse · doi:10.1002/syn.21642 · Cited by 23
Direct Observation of Aggregation‐Induced Backbone Conformational Changes in Tau Peptides
Jiji, A. C., Shine, A., & Vijayan, V. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201606544 · Cited by 22
McDaid, J., Briggs, C. A., Barrington, N. M., Peterson, D. A., Kozlowski, D. A., & Stutzmann, G. E. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.652721 · Cited by 22
Cerebrospinal fluid microRNAs as potential biomarkers in Alzheimer’s disease
Eddin, A. N., Hamsho, K., Adi, G., Al-Rimawi, M., Alfuwais, M., Rab, S. A., AlKattan, K. M., & Yaqinuddin, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1210191 · Cited by 26
Li, K., Jia, H.-C., She, X., Cui, B., Zhang, N., Chen, X., Xu, C.-X., An, G., & Ma, Q. (2014) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2014.03.027 · Cited by 22
Lee‐Chen, G., Chang, K.-H., Chen, I., Lin, H.-Y., Chen, H.-C., Lin, C., Lin, T., Weng, Y.-T., Chao, C., Wu, Y.-R., et al. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s96454 · Cited by 22
Beckelman, B. C., Day, S. M., Zhou, X., Donohue, M., Gouras, G. K., Klann, E., Keene, C. D., & Ma, T. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160036 · Cited by 29
Elucidating Critical Proteinopathic Mechanisms and Potential Drug Targets in Neurodegeneration
Dar, K. B., Bhat, A. H., Amin, S., Reshi, B. A., Zargar, M. A., Masood, A., & Ganie, S. A. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00741-0 · Cited by 23
Compartmental protein expression of Tau, GSK-3β and TrkA in cholinergic neurons of aged rats
Niewiadomska, G., Baksalerska-Pazera, M., Lenarcik, I., & Riedel, G. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0488-4 · Cited by 22
Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 27
Brain Damage - Bridging Between Basic Research and Clinics
González-Quevedo, A. (2012) · InTech eBooks · doi:10.5772/2174 · Cited by 21
Astrocytes in Neurodegenerative Diseases: A Perspective from Tauopathy and α-Synucleinopathy
Wang, P., & Ye, Y. (2021) · Life · doi:10.3390/life11090938 · Cited by 21
Alaouy, M. A. E., Alaqarbeh, M., Ouabane, M., Zaki, H., ElBouhi, M., Badaoui, H., Moukhliss, Y., Sbai, A., Maghat, H., Lakhlifi, T., et al. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2252116 · Cited by 21
Li, L., Peng, Y., Hui, Y., Zhang, S., Zhou, Y. L., Li, D., Li, J., Si, Z., Li, J., Wang, D., et al. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150027 · Cited by 22
Posterior cingulate cortex reveals an expression profile of resilience in cognitively intact elders
Kelley, C. M., Ginsberg, S. D., Liang, W. S., Counts, S., & Mufson, E. J. (2022) · Brain Communications · doi:10.1093/braincomms/fcac162 · Cited by 23
New Age of Neuroproteomics in Alzheimer’s Disease Research
Kováčech, B., Žilka, N., & Novák, M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9358-6 · Cited by 22
Metadata
- Authors
- Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., Tanimukai, H., & Grundke-Iqbal, I.
- Affiliations
- New York State Office for People With Developmental Disabilities (US)
- Corresponding author
- Iqbal, Khalid
- ORCID
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2005-01
- Volume
- 1739
- Issue
- 2-3
- Pages
- 198-210
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W1998440070
- Cited by
- 1,037
- References
- 154
- Citations by year
- 2026: 28 · 2025: 48 · 2024: 50 · 2023: 67 · 2022: 60 · 2021: 60 · 2020: 57 · 2019: 58 · 2018: 64 · 2017: 48 · 2016: 48 · 2015: 54 · 2014: 52 · 2013: 48 · 2012: 52
- FWCI
- 3.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG19158, R01AG019158)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tauopathy, Alzheimer's disease, tau hyperphosphorylation, neurofibrillary tangles, paired helical filaments, microtubule stabilization, MAP2, tau kinases, protein phosphatase 2A, frontotemporal dementia, tau conformation, neurodegeneration, tau dephosphorylation, tau-targeted therapy
- MeSH terms
- Alzheimer Disease, Brain, Enzyme Inhibitors, Humans, Models, Biological, Nerve Degeneration, Neurofibrils, Phosphoprotein Phosphatases, Phosphorylation, Protein Conformation, Protein Kinases, Neurofibrillary Tangles, tau Proteins, Tauopathies, Protein Phosphatase 2
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