Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
Abstract
Abnormally phosphorylated tau proteins (A68) are the building blocks of Alzheimer's disease (AD) paired helical filaments. The biological consequences of the conversion of normal adult tau to A68 remain unknown. Here we demonstrate that native A68 does not bind to microtubules (MTs), yet dephosphorylated A68 regains the ability to bind to MTs. Ser396 is phosphorylated in A68, but not in normal adult tau, whereas fetal tau is phosphorylated transiently at this site. Phosphorylation of tau at Ser396 by protein kinases in CHO cells and rat brain produces an electrophoretic mobility similar to that of A68. Using CHO cells transfected with an Ala396 mutant, we show that the phosphorylation of tau at Ser396 reduces its affinity for MTs and its ability to stabilize MTs against nocodazole-induced depolymerization. Our results demonstrate that the abnormal phosphorylation of tau in AD involves Ser396, and we suggest that this may be mediated by the inappropriate activation of fetal kinases or the reduced activity of tau protein phosphatases. Thus, phosphorylation of Ser396 may destabilize MTs in AD, resulting in the degeneration of affected cells.
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Many phosphorylated residues in PHF-tau are serines or threonines followed by proline.
“Prior studies have shown that many phosphorylated residues in PHF-tau are serines or threonines followed by a proline [1,6,8,11].”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [1]
The CHO T44 and CHO T40 cell lines stably expressing tau had >95% of cells expressing high levels of the tau proteins.
“CHO cell lines stably expressing either three-repeat tau (CHO T44) or two N-terminal insert four-repeat tau (CHO T40) were prepared as described [1] and >95% of the CHO T44 and CHO T40 cells express high levels of these tau proteins.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [1]
Tau phosphorylated at S396 is found in paired helical filaments.
“S199 and T231 are two of the earliest phosphorylated sites on tau in AD (Maurage et al., 2003, Luna-Munoz et al., 2007), and tau phosphorylated at S396 is found in paired helical filaments (Bramblett et al., 1993).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Bramblett et al., 1993
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- Authors
- Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y.
- Affiliations
- University of Pennsylvania (US)
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 10
- Issue
- 6
- Pages
- 1089-1099
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1973774127
- Cited by
- 903
- References
- 6
- Citations by year
- 2026: 16 · 2025: 25 · 2024: 30 · 2023: 28 · 2022: 28 · 2021: 26 · 2020: 38 · 2019: 25 · 2018: 24 · 2017: 20 · 2016: 33 · 2015: 25 · 2014: 26 · 2013: 27 · 2012: 27
- FWCI
- 26.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › 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 phosphorylation, Alzheimer's disease, microtubule binding, paired helical filaments, microtubule stabilization, neurodegeneration
- MeSH terms
- Adult, Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cerebral Cortex, Fetus, Cricetinae, Humans, Microtubules, Phosphorylation, Phosphoserine, Protein Binding, Recombinant Proteins, Serine, Transfection, CHO Cells, tau Proteins, Rats
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