Evidence map›Paper›PMID 32585685›Full record

ArticleThe Journal of cell biology2020

Topological features of integrin adhesion complexes revealed by multiplexed proximity biotinylation.

Megan R Chastney, Craig Lawless, Jonathan D Humphries, Stacey Warwood, Matthew C Jones, David Knight, Claus Jorgensen, Martin J Humphries

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. How Neuromorphic Microstructures Control In Vitro Early-Stage Neuronal Outgrowth.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  13. Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024
    Review
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  18. Review
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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

8 authors at 1 institution in 1 country.

Megan R ChastneyWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Craig LawlessWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Jonathan D HumphriesWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Stacey WarwoodBiological Mass Spectrometry Core Facility, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Matthew C JonesWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
David KnightBiological Mass Spectrometry Core Facility, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Claus JorgensenCancer Research UK Manchester Institute, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Alderley Park, Manchester, UK.
Martin J HumphriesWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine & Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, UK.
Manchester Academic Health Science Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D008719/1Cancer Research UK 19258Cancer Research UK 21671Cancer Research UK A19258Cancer Research UK A25236Cancer Research UK C13329/A21671Wellcome TrustWellcome Trust 203128/Z/16/Z
6 · The paper itself

Abstract

Integrin adhesion complexes (IACs) bridge the extracellular matrix to the actin cytoskeleton and transduce signals in response to both chemical and mechanical cues. The composition, interactions, stoichiometry, and topological organization of proteins within IACs are not fully understood. To address this gap, we used multiplexed proximity biotinylation (BioID) to generate an in situ, proximity-dependent adhesome in mouse pancreatic fibroblasts. Integration of the interactomes of 16 IAC-associated baits revealed a network of 147 proteins with 361 proximity interactions. Candidates with underappreciated roles in adhesion were identified, in addition to established IAC components. Bioinformatic analysis revealed five clusters of IAC baits that link to common groups of prey, and which therefore may represent functional modules. The five clusters, and their spatial associations, are consistent with current models of IAC interaction networks and stratification. This study provides a resource to examine proximal relationships within IACs at a global level.

Indexed as

Cell AdhesionProteomicsActin CytoskeletonAnimalsBiotinylationCell LineChromatography, High Pressure LiquidComputational BiologyExtracellular MatrixFibroblastsIntegrinsMicePancreasProtein Interaction MapsSignal TransductionTandem Mass SpectrometryIntegrins

Identifiers

PMID32585685
PMCPMC7401799
OpenAlexW3037011268

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.