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Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains
Open accessAbstract
It is widely believed that tau stabilizes microtubules in the axon [1-3] and, hence, that disease-induced loss of tau from axonal microtubules leads to their destabilization [3-5]. An individual microtubule in the axon has a stable domain and a labile domain [6-8]. We found that tau is more abundant on the labile domain, which is inconsistent with tau's proposed role as a microtubule stabilizer. When tau is experimentally depleted from cultured rat neurons, the labile microtubule mass of the axon drops considerably, the remaining labile microtubule mass becomes less labile, and the stable microtubule mass increases. MAP6 (also called stable tubule-only polypeptide), which is normally enriched on the stable domain [9], acquires a broader distribution across the microtubule when tau is depleted, providing a potential explanation for the increase in stable microtubule mass. When MAP6 is depleted, the labile microtubule mass becomes even more labile, indicating that, unlike tau, MAP6 is a genuine stabilizer of axonal microtubules. We conclude that tau is not a stabilizer of axonal microtubules but is enriched on the labile domain of the microtubule to promote its assembly while limiting the binding to it of genuine stabilizers, such as MAP6. This enables the labile domain to achieve great lengths without being stabilized. These conclusions are contrary to tau dogma.
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“The actual role of tau in regulating microtubule stability in the axon is not to stabilise axonal microtubules, but rather to allow them to have long labile domains [16,17].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [17]
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Multifunctional Protein Tau Aggregation and Cytotoxicity
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Injury-induced tau pathology promotes aggressive behavior in Drosophila without neurodegenerationPreprint
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Additional file 1 of Mical modulates Tau toxicity via cysteine oxidation in vivo
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Metadata
- Authors
- Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W.
- Affiliations
- Nantong University (CN)
- Drexel University (US)
- Corresponding author
- Qiang, Liang
- Baas, Peter W.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2018-07
- Volume
- 28
- Issue
- 13
- Pages
- 2181-2189.e4
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2810622900
- Cited by
- 222
- References
- 46
- Citations by year
- 2026: 20 · 2025: 22 · 2024: 18 · 2023: 26 · 2022: 26 · 2021: 43 · 2020: 35 · 2019: 24 · 2018: 8
- FWCI
- 18.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- NIH (R01 NS28785)
- US Department of Defense (W81XWH-17-1-0504)
- Pennsylvania Department of Health CURE program
- National Natural Science Foundation of China (31371078)
- Natural Science Foundation of Jiangsu Province (BK20171253)
- Brody Family Medical Trust Fund
- National Science Foundation Graduate Research Fellowship (1002809)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, axonal microtubules, microtubule stabilization, MAP6, microtubule assembly, tauopathy, axons
- MeSH terms
- Animals, Axons, Cells, Cultured, Microtubules, tau Proteins, Rats, Sprague-Dawley, Rats
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