Evidence map›Paper›PMID 15272303›Full record

ArticleThe EMBO journal2004

Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle.

Evangelos Papagrigoriou, Alexandre R Gingras, Igor L Barsukov, Neil Bate, Ian J Fillingham, Bipin Patel, Ronald Frank, Wolfgang H Ziegler, Gordon C K Roberts, David R Critchley and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

90 citing papers in PubMed, 170 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Allosteric activation of vinculin by talin.Nature communications · 2023
    Article
  13. Article
  14. Review
  15. Viscoelasticity, Like Forces, Plays a Role in Mechanotransduction.Frontiers in cell and developmental biology · 2022
    Review
  16. Article
  17. Article
  18. Mechanoregulation of PDZ Proteins, An Emerging Function.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  19. Article
  20. Article

30 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

11 authors at 4 institutions in 2 countries.

Evangelos PapagrigoriouDepartment of Biochemistry, University of Leicester, Leicester, UK.
Alexandre R Gingras
Igor L Barsukov
Neil Bate
Ian J Fillingham
Bipin Patel
Ronald Frank
Wolfgang H Ziegler
Gordon C K Roberts
David R Critchley
Jonas Emsley
University of Leicester · GBHelmholtz Centre for Infection Research · DETechnische Universität Braunschweig · DEUniversity of Nottingham · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482-789. Talin 482-655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656-789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions.

Indexed as

Amino Acid SequenceAnimalsBinding SitesChickensHydrophobic and Hydrophilic InteractionsLigandsModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein Array AnalysisProtein BindingProtein FoldingProtein Structure, TertiarySequence AlignmentTalinLigandsTalinVinculin

Identifiers

PMID15272303
PMCPMC514914
OpenAlexW2147898539

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.