Hyperphosphorylation of Tau Associates With Changes in Its Function Beyond Microtubule Stability
Open accessAbstract
Tau is a neuronal microtubule associated protein whose main biological functions are to promote microtubule self-assembly by tubulin and to stabilize those already formed. Tau also plays an important role as an axonal microtubule protein. Tau is an amazing protein that plays a key role in cognitive processes, however, deposits of abnormal forms of tau are associated with several neurodegenerative diseases, including Alzheimer disease (AD), the most prevalent, and Chronic Traumatic Encephalopathy (CTE) and Traumatic Brain Injury (TBI), the most recently associated to abnormal tau. Tau post-translational modifications (PTMs) are responsible for its gain of toxic function. Alonso et al. (1996) were the first to show that the pathological tau isolated from AD brains has prion-like properties and can transfer its toxic function to the normal molecule. Furthermore, we reported that the pathological changes are associated with tau phosphorylation at Ser199 and 262 and Thr212 and 231. This pathological version of tau induces subcellular mislocalization in cultured cells and neurons, and translocates into the nucleus or accumulated in the perinuclear region of cells. We have generated a transgenic mouse model that expresses pathological human tau (PH-Tau) in neurons at two different concentrations (4% and 14% of the total endogenous tau). In this model, PH-Tau causes cognitive decline by at least two different mechanisms: one that involves the cytoskeleton with axonal disruption (at high concentration), and another in which the apparent neuronal morphology is not grossly affected, but the synaptic terminals are altered (at lower concentration). We will discuss the putative involvement of tau in proteostasis under these conditions. Understanding tau's biological activity on and off the microtubules will help shed light to the mechanism of neurodegeneration and of normal neuronal function.
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Tau phosphorylation at specific sites overlapping AD sites diminishes tau's affinity for microtubules.
“It is well established that tau phosphorylation, especially at specific sites that overlap with the sites that are phosphorylated in AD, diminishes the affinity of tau for microtubules (4, 26–29).”
From All the Tau We Cannot See (2023) · cites this paper as [26]
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Self-citationThe Tau Misfolding Pathway to Dementia
Alonso, A. D. C., Cohen, L. S., & Morozova, V. (2017) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789813222960_0004 · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Baquero J. Ordonez M. Alonso A. D. Kleinman F. E. (2015). “ Tau phosphorylation plays a role in mRNA 3′ end processing,” in Proceedings of the 4th Metabolism in Neurological Disease and 11th Brain Research Conference, Society for Neuroscience, New York, NY.
Cited by
Sorted by citations
Inflammation in obesity, diabetes, and related disorders
Rohm, T. V., Meier, D. T., Olefsky, J. M., & Donath, M. Y. (2022) · Immunity · doi:10.1016/j.immuni.2021.12.013 · Cited by 2,066 · see citing works
Role of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works
De Simone, A., Tumiatti, V., Andrisano, V., & Milelli, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00931 · Cited by 110 · see citing works
Hyman, B. (2023) · Annual Review of Medicine · doi:10.1146/annurev-med-042921-023749 · Cited by 39 · see citing works
HMGCS2-Induced Autophagic Degradation of Tau Involves Ketone Body and ANKRD24
Hu, L.-T., Xie, X.-Y., Zhou, G.-F., Wen, Q.-X., Song, L., Luo, B., Deng, X.-J., Pan, Q.-L., & Chen, G.-J. (2023) · Journal of Alzheimer's Disease · doi:10.3233/jad-220640 · Cited by 14 · see citing works
- Authors
- Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., & Kleiman, F. E.
- Affiliations
- The Graduate Center, CUNY (US)
- College of Staten Island (US)
- Wagner College (US)
- Corresponding author
- Alonso, Alejandra D.
- Venue
- Frontiers in Cellular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2018-10-09
- Volume
- 12
- Pages
- 338-338
- ISSN
- 1662-5102 (ISSN-L)
- PMC
- PMC6189415
- OpenAlex
- W2896801782
- Cited by
- 278
- References
- 82
- Citations by year
- 2026: 39 · 2025: 38 · 2024: 34 · 2023: 32 · 2022: 51 · 2021: 35 · 2020: 35 · 2019: 13 · 2018: 1
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CUNY Academic Works (City University of New York) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Institutes of Health (R15AG034524-01, 1R15AG058197-01)
- Alzheimer’s Association (IIRG-09-133206)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau hyperphosphorylation, pathological tau, Alzheimer's disease, chronic traumatic encephalopathy, traumatic brain injury, transgenic mouse model, cognitive decline, axonal disruption, synaptic terminals, proteostasis, neurodegeneration, microtubule stability
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