Evidence map›Paper›PMID 17932487›Full record

ArticleThe EMBO journal2007

Interaction of tau protein with the dynactin complex.

Enrico Magnani, Juan Fan, Laura Gasparini, Matthew Golding, Meredith Williams, Giampietro Schiavo, Michel Goedert, Linda A Amos, Maria Grazia Spillantini

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
7.5field-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

97 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. A Validated Method to Prepare Stable Tau Oligomers.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction.International journal of molecular sciences · 2021
    Review
  17. Review
  18. Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.Protein science : a publication of the Protein Society · 2021
    Review
  19. Article
  20. Insights into Disease-Associated Tau Impact on Mitochondria.International journal of molecular sciences · 2020
    Review

37 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

9 authors at 3 institutions in 1 country.

Enrico MagnaniDepartment of Clinical Neurosciences, Brain Repair Centre, University of Cambridge, Cambridge, UK.
Juan Fan
Laura Gasparini
Matthew Golding
Meredith Williams
Giampietro Schiavo
Michel Goedert
Linda A Amos
Maria Grazia Spillantini
University of Cambridge · GBMedical Research Council · GBCancer Research UK · GB

Funding

Medical Research Council G0301152Medical Research Council MC_U105184291Medical Research Council MC_U105184313Medical Research Council U.1051.04.002(78842)
6 · The paper itself

Abstract

Tau is an axonal microtubule-associated protein involved in microtubule assembly and stabilization. Mutations in Tau cause frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), and tau aggregates are present in Alzheimer's disease and other tauopathies. The mechanisms leading from tau dysfunction to neurodegeneration are still debated. The dynein-activator complex dynactin has an essential role in axonal transport and mutations in its gene are associated with lower motor neuron disease. We show here for the first time that the N-terminal projection domain of tau binds to the C-terminus of the p150 subunit of the dynactin complex. Tau and dynactin show extensive colocalization, and the attachment of the dynactin complex to microtubules is enhanced by tau. Mutations of a conserved arginine residue in the N-terminus of tau, found in patients with FTDP-17, affect its binding to dynactin, which is abnormally distributed in the retinal ganglion cell axons of transgenic mice expressing human tau with a mutation in the microtubule-binding domain. These findings, which suggest a direct involvement of tau in axonal transport, have implications for understanding the pathogenesis of tauopathies.

Indexed as

AnimalsArginineAxonsCloning, MolecularDynactin ComplexHumansMiceMicrotubule-Associated ProteinsModels, BiologicalMutationNeuronsParkinsonian DisordersProtein BindingProtein Structure, Tertiarytau ProteinsTwo-Hybrid System TechniquesArginineDynactin ComplexMicrotubule-Associated Proteinstau Proteins

Identifiers

PMID17932487
PMCPMC2063488
OpenAlexW2119598236

What OpenQuestion holds

Textmetadata
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.