Evidence map›Paper›PMID 20150896›Full record

ArticleThe EMBO journal2010

Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation.

Benjamin T Goult, Mohamed Bouaouina, Paul R Elliott, Neil Bate, Bipin Patel, Alexandre R Gingras, J Günter Grossmann, Gordon C K Roberts, David A Calderwood, David R Critchley and 1 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
6.8field-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

103 citing papers in PubMed, 145 citations in OpenAlex.

  1. Review
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  5. The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. [Molecular dynamics simulation of force-regulated interaction between talin and Rap1b].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2023
    Article
  11. Review
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43 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 3 institutions in 2 countries.

Benjamin T GoultDepartment of Biochemistry, University of Leicester, Leicester, UK.
Mohamed Bouaouina
Paul R Elliott
Neil Bate
Bipin Patel
Alexandre R Gingras
J Günter Grossmann
Gordon C K Roberts
David A Calderwood
David R Critchley
Igor L Barsukov
University of Leicester · GBUniversity of Liverpool · GBYale University · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
Integrin-Filamin Interactions in Migration and SignalingR01GM068600 · NIGMS · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2003 to 2016
$4.4M
Identification of beta 1 integrin activating proteinsR21HL089433 · NHLBI · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2007 to 2008
$454k
Biotechnology and Biological Sciences Research Council BB/G003637/1Cancer Research UKNHLBI NIH HHS R21 HL089433NIGMS NIH HHS R01 GM068600NIGMS NIH HHS U54 GM064346NIGMS NIH HHS U54 GM64346Wellcome Trust
6 · The paper itself

Abstract

Talin is a 270-kDa protein that activates integrins and couples them to cytoskeletal actin. Talin contains an N-terminal FERM domain comprised of F1, F2 and F3 domains, but it is atypical in that F1 contains a large insert and is preceded by an extra domain F0. Although F3 contains the binding site for beta-integrin tails, F0 and F1 are also required for activation of beta1-integrins. Here, we report the solution structures of F0, F1 and of the F0F1 double domain. Both F0 and F1 have ubiquitin-like folds joined in a novel fixed orientation by an extensive charged interface. The F1 insert forms a loop with helical propensity, and basic residues predicted to reside on one surface of the helix are required for binding to acidic phospholipids and for talin-mediated activation of beta1-integrins. This and the fact that basic residues on F2 and F3 are also essential for integrin activation suggest that extensive interactions between the talin FERM domain and acidic membrane phospholipids are required to orientate the FERM domain such that it can activate integrins.

Indexed as

Amino Acid SequenceBinding SitesCell AdhesionIntegrinsModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryTalinUbiquitinIntegrinsTalinUbiquitin

Identifiers

PMID20150896
PMCPMC2845276
OpenAlexW2032348507

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.