Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.
Open accessAbstract
The microtubule assembly-promoting activity of different pools of tau protein isolated from Alzheimer disease (AD) and control brains and the effect of dephosphorylation on this activity were studied. Tau isolated from a 2.5% perchloric extract of AD brain had almost the same activity as that obtained from control brain, and this activity did not change significantly on dephosphorylation. Abnormally phosphorylated tau (AD P-tau) isolated from brain homogenate of AD patients had little activity, and upon dephosphorylation with alkaline phosphatase, its activity increased to approximately the same level as the acid-soluble tau. Addition of AD P-tau to a mixture of normal tau and tubulin inhibited microtubule assembly. AD P-tau bound to normal tau but not to tubulin. These studies suggest that the abnormal phosphorylation of tau might be responsible for the breakdown of microtubules in affected neurons in AD not only because the altered protein has little microtubule-promoting activity but also because it interacts with normal tau, making the latter unavailable for promoting the assembly of tubulin into microtubules.
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Tau proteins in Alzheimer's disease are hyperphosphorylated and abnormally folded compared to unassembled normal tau, and they have lost their normal abilities to bind and stabilize microtubules in the axon.
“Tau proteins in AD are hyperphosphorylated and abnormally folded compared to unassembled normal tau, and they have lost their normal abilities to bind and stabilize microtubules in the axon [60].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [60]
The Abstract reports that abnormally phosphorylated tau from AD brain had little microtubule assembly-promoting activity and bound normal tau rather than tubulin. It does not establish that AD tau is abnormally folded, compare it with “unassembled normal tau,” or specifically demonstrate loss of microtubule stabilization in axons. It also reports that another pool of AD tau had nearly normal assembly-promoting activity. (LLM, conf=0.86)
Experimental — accuracy not yet measuredTau hyperphosphorylation increases Tau's propensity to form aggregates.
“and increases its propensity to form aggregates [6].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [6]
The available Abstract reports that abnormally phosphorylated tau binds normal tau and inhibits microtubule assembly, but it does not say phosphorylation increases tau aggregate formation. Searches for aggregation and self-association found only reference titles, not a finding in this paper; the article’s main text is not available as searchable text in our copy. (LLM, conf=0.72)
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- Authors
- Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K.
- Affiliations
- New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.
- ORCID
- Zaidi, T
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-06-07
- Volume
- 91
- Issue
- 12
- Pages
- 5562-5566
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44036
- OpenAlex
- W1964927978
- Cited by
- 738
- References
- 3
- Citations by year
- 2026: 12 · 2025: 20 · 2024: 27 · 2023: 38 · 2022: 38 · 2021: 42 · 2020: 43 · 2019: 35 · 2018: 34 · 2017: 31 · 2016: 30 · 2015: 17 · 2014: 36 · 2013: 21 · 2012: 21
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- McLean Hospital
- National Institutes of Health (5r01ag008076-09, 5r01ag005892-16, 5r01ns018105-17)
- National Institute on Aging (AG-05892, AG 08076)
- National Institute of Neurological Disorders and Stroke (NS 18105)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, Alzheimer's disease, microtubule assembly, dephosphorylation, tubulin, protein-protein interaction, alkaline phosphatase
- MeSH terms
- Alzheimer Disease, Animals, Cytosol, Humans, Microtubules, Phosphoproteins, Phosphorylation, Protein Binding, Tubulin, tau Proteins, Rats, In Vitro Techniques
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