Evidence map›Paper›PMID 26935805›Full record

ArticleNature communications2016

Mechanism of intermediate filament recognition by plakin repeat domains revealed by envoplakin targeting of vimentin.

Claudia Fogl, Fiyaz Mohammed, Caezar Al-Jassar, Mark Jeeves, Timothy J Knowles, Penelope Rodriguez-Zamora, Scott A White, Elena Odintsova, Michael Overduin, Martyn Chidgey

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. A CaCells · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Recent insight into intermediate filament structure.Current opinion in cell biology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Biomedical potential of mammalian spectraplakin proteins: Progress and prospect.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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

10 authors at 1 institution in 1 country.

Claudia FoglSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Fiyaz MohammedInstitute of Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, UK.
Caezar Al-JassarSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Mark JeevesSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Timothy J KnowlesSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Penelope Rodriguez-ZamoraNanoscale Physics Research Laboratory, School of Physics and Astronomy, University of Birmingham, Birmingham B15 2TT, UK.
Scott A WhiteSchool of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
Elena OdintsovaInstitute of Cancer and Genomic Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Michael OverduinSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Martyn ChidgeySchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
University of Birmingham · GB

Funding

Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Plakin proteins form critical connections between cell junctions and the cytoskeleton; their disruption within epithelial and cardiac muscle cells cause skin-blistering diseases and cardiomyopathies. Envoplakin has a single plakin repeat domain (PRD) which recognizes intermediate filaments through an unresolved mechanism. Herein we report the crystal structure of envoplakin's complete PRD fold, revealing binding determinants within its electropositive binding groove. Four of its five internal repeats recognize negatively charged patches within vimentin via five basic determinants that are identified by nuclear magnetic resonance spectroscopy. Mutations of the Lys1901 or Arg1914 binding determinants delocalize heterodimeric envoplakin from intracellular vimentin and keratin filaments in cultured cells. Recognition of vimentin is abolished when its residues Asp112 or Asp119 are mutated. The latter slot intermediate filament rods into basic PRD domain grooves through electrosteric complementarity in a widely applicable mechanism. Together this reveals how plakin family members form dynamic linkages with cytoskeletal frameworks.

Indexed as

Amino Acid MotifsAnimalsCloning, MolecularEscherichia coliHumansIntermediate FilamentsMembrane ProteinsModels, MolecularPhylogenyProtein BindingProtein ConformationProtein PrecursorsVimentinenvoplakinMembrane ProteinsProtein PrecursorsVimentin

Identifiers

PMID26935805
PMCPMC4782060
OpenAlexW2294569491

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.