Evidence map›Paper›PMID 33398028›Full record

ArticleNature communications2021

Filamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex.

Peng Wang, Yihong Ye

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
6.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. BAG3 modulates clathrin-mediated endocytosis and tau uptake in astrocytes.American journal of physiology. Cell physiology · 2026
    Article
  6. Review
  7. Review
  8. Article
  9. Article
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  12. Protective mechanisms against Alzheimer's disease in APOE3-Christchurch homozygous astrocytes.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Astrocyte and oligodendrocyte pathology in Alzheimer's disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  18. Article
  19. Article
  20. Review

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Peng WangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Yihong YeLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA. yihongy@mail.nih.gov.ORCID 0000-0002-9512-7922
National Institutes of Health · US

Funding

Unconventional protein secretion-mediated protein quality control in health and diseasesZIADK075143 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2017 to 2025
$6.7M
6 · The paper itself

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.

Indexed as

AnimalsAstrocytesCells, CulturedFocal Adhesion Protein-Tyrosine KinasesHEK293 CellsHeparan Sulfate ProteoglycansHumansInflammationMiceMice, Inbred C57BLNeuronsNF-kappa BProtein BindingReceptors, VitronectinRecombinant ProteinsSignal TransductionFocal Adhesion Protein-Tyrosine KinasesHeparan Sulfate Proteoglycansintegrin alphavbeta1NF-kappa BReceptors, VitronectinRecombinant ProteinsSTAT3 Transcription FactorTalintau Proteins

Identifiers

PMID33398028
PMCPMC7782792
OpenAlexW3118652952

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.