Microtubule destruction induces tau liberation and its subsequent phosphorylation
Abstract
Neurofibrillary tangle‐bearing neurons, a pathological hallmark of Alzheimer's disease, are mostly devoid of normal microtubule (MT) structure and instead have paired helical filaments that are composed of abnormal hyperphosphorylated tau. However, a causal relationship between tau phosphorylation and MT disruption has not been clarified. To examine whether MT disruption induces tau phosphorylation, stathmin, an MT‐disrupting protein, was co‐expressed with tau in COS‐7 cells. Stathmin expression induced apparent MT catastrophe and tau hyperphosphorylation at Thr‐181, Ser‐202, Thr‐205, and Thr‐231 sites. In contrast, c‐Jun N‐terminal kinase activation, or phosphatase inhibition, led to significant tau phosphorylation without affecting MT structure. These findings suggest that MT disruption induces subsequent tau phosphorylation.
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Chronic neuroinflammation could provoke tau pathology thereby worsening neuronal injury and long-term outcome.
“Together, these studies indicate that chronic neuroinflammation could provoke tau pathology thereby worsening neuronal injury and long-term outcome.”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [151]
A robust and persistent neuroinflammatory response may be sufficient to promote phosphorylation, aggregation, and subsequent neurodegeneration; key features of AD.
“A robust and persistent neuroinflammatory response may then be sufficient to promote phosphorylation, aggregation, and subsequent neurodegeneration; key features of AD (149–151).”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [151]
Tau proteins detached from microtubules are prone to be phosphorylated at disease-associated sites.
“tau proteins detached from microtubules are prone to be phosphorylated at disease-associated sites [19, 25–28].”
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References 48 · Cited by 41
- Authors
- Miyasaka, T., Sato, S., Tatebayashi, Y., & Takashima, A.
- Affiliations
- Doshisha University (JP)
- RIKEN Center for Brain Science (JP)
- Corresponding author
- Miyasaka, Tomohiro
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2010-06-16
- Volume
- 584
- Issue
- 14
- Pages
- 3227-3232
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2042171021
- Cited by
- 41
- References
- 48
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 5 · 2018: 4 · 2017: 2 · 2016: 7 · 2015: 1 · 2014: 3 · 2013: 3 · 2012: 3
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- JSPS KAKENHI
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- microtubule disruption, tau phosphorylation, stathmin, neurofibrillary tangles, Alzheimer's disease, microtubule catastrophe, c-Jun N-terminal kinase, phosphatase inhibition, paired helical filaments
- MeSH terms
- Alzheimer Disease, Animals, Chlorocebus aethiops, Cytoskeletal Proteins, Enzyme Inhibitors, Mice, Transgenic, Microtubules, Neurons, Phosphorylation, Neurofibrillary Tangles, tau Proteins, COS Cells, JNK Mitogen-Activated Protein Kinases, Mice
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