Evidence map›Paper›PMID 19798053›Full record

ArticleThe EMBO journal2009

The structure of an integrin/talin complex reveals the basis of inside-out signal transduction.

Nicholas J Anthis, Kate L Wegener, Feng Ye, Chungho Kim, Benjamin T Goult, Edward D Lowe, Ioannis Vakonakis, Neil Bate, David R Critchley, Mark H Ginsberg and 1 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

203 citing papers in PubMed, 340 citations in OpenAlex.

  1. Article
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  8. Review
  9. Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
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  14. Review
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  16. Phagocytosis by the retinal pigment epithelium: New insights into polarized cell mechanics.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

143 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.

Nicholas J AnthisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. nick.anthis@gmail.com
Kate L Wegener
Feng Ye
Chungho Kim
Benjamin T Goult
Edward D Lowe
Ioannis Vakonakis
Neil Bate
David R Critchley
Mark H Ginsberg
Iain D Campbell
University of California, San Diego · USUniversity of Leicester · GBUniversity of Oxford · GB

Funding

The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
Regulation of Integrin Alpha4 BetalR01AR027214 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 1986 to 2010
$3.5M
PLATELETS IN RHEUMATIC DISEASER37AR027214 · NIAMS · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1991 to 2000
$279k
Cancer Research UKNHLBI NIH HHS HL078784NHLBI NIH HHS P01 HL078784NIAMS NIH HHS AR27214NIAMS NIH HHS R01 AR027214NIAMS NIH HHS R37 AR027214Wellcome Trust
6 · The paper itself

Abstract

Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the beta integrin subunit. Here, we report the first structure of talin bound to an authentic full-length beta integrin tail. Using biophysical and whole cell measurements, we show that a specific ionic interaction between the talin F3 domain and the membrane-proximal helix of the beta tail disrupts an integrin alpha/beta salt bridge that helps maintain the integrin inactive state. Second, we identify a positively charged surface on the talin F2 domain that precisely orients talin to disrupt the heterodimeric integrin transmembrane (TM) complex. These results show key structural features that explain the ability of talin to mediate inside-out TM signalling.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCell PolarityCHO CellsCricetinaeCricetulusIntegrinsMacromolecular SubstancesModels, BiologicalModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidSignal TransductionIntegrinsMacromolecular SubstancesTalin

Identifiers

PMID19798053
PMCPMC2782098
OpenAlexW2118758577

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.