Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex
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Abstract
Microtubule-associated protein Tau can form protein aggregates transmissible within the brain, correlating with the progression of tauopathies in humans. The transmission of aggregates requires neuron-released Tau to interact with surface receptors on target cells. However, the underlying molecular mechanisms in astrocytes and downstream effects are unclear. Here, using a spatially resolved proteomic mapping strategy, we show that integrin αV/β1 receptor binds recombinant human Tau, mediating the entry of Tau fibrils in astrocytes. The binding of distinct Tau species to the astrocytic αV/β1 receptor differentially activate integrin signaling. Furthermore, Tau-mediated activation of integrin signaling results in NFκB activation, causing upregulation of pro-inflammatory cytokines and chemokines, induction of a sub-group of neurotoxic astrocytic markers, and release of neurotoxic factors. Our findings suggest that filamentous recombinant human Tau-mediated activation of integrin signaling induces astrocyte conversion towards a neurotoxic state, providing a mechanistic insight into tauopathies.
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Astrocytes can internalize both tau monomers and higher-molecular-weight tau species.
“Previous studies have demonstrated that astrocytes can internalize both tau monomers and higher‐molecular‐weight tau species. 13 , 28”
From Protective mechanisms against Alzheimer's disease in APOE3‐Christchurch homozygous astrocytes (2025) · cites this paper as [28]
The Results section, “HSPG-independent uptake of Tau PFFs by primary astrocytes,” reports efficient internalization of tau fibrils by primary astrocytes. It says the cells were also treated with monomeric tau, but does not report that they internalized it. The Introduction broadly mentions uptake of different tau species by neurons, microglia, and astrocytes without establishing monomer uptake specifically in astrocytes. (LLM, conf=0.85)
Experimental — accuracy not yet measuredBinding of tau fibrils to astrocyte αV/β1 activates integrin signaling, resulting in NF-κB activation, leading to an increase of pro-inflammatory cytokines and chemokines, and induction of expression of neurotoxic astrocytic markers.
“The binding of tau fibrils to astrocyte αV/β1 activates integrin signaling, resulting in NF-κB activation, leading to an increase of pro-inflammatory cytokines and chemokines, and induction of expression of neurotoxic astrocytic markers [203].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [203]
The integrin αV/β1 receptor interacts with tau monomers or fibrils and mediates tau uptake in primary astrocytes.
“The integrin αV/β1 receptor interacts with tau monomers or fibrils and mediates tau uptake in primary astrocytes.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [203]
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- Authors
- Wang, P., & Ye, Y.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Ye, Yihong
- ORCID
- Venue
- Nature Communications
- Published
- 2021-01-04
- Volume
- 12
- Issue
- 1
- Pages
- 95-95
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC7782792
- OpenAlex
- W3118652952
- Cited by
- 93
- References
- 75
- Citations by year
- 2026: 11 · 2025: 19 · 2024: 17 · 2023: 15 · 2022: 20 · 2021: 10 · 2020: 1
- FWCI
- 10.98
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- tau protein, tauopathy, astrocytes, integrin αvβ1, integrin signaling, tau fibrils, NF-κB activation, inflammatory cytokines, chemokines, neuroinflammation
- MeSH terms
- Animals, Astrocytes, Cells, Cultured, Humans, Inflammation, Mice, Inbred C57BL, Neurons, Protein Binding, Recombinant Proteins, Signal Transduction, NF-kappa B, Talin, tau Proteins, Receptors, Vitronectin, Heparan Sulfate Proteoglycans, STAT3 Transcription Factor, Mice, Focal Adhesion Protein-Tyrosine Kinases, HEK293 Cells
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