Evidence map›Paper›PMID 27737911›Full record

ArticleJournal of cell science2016

Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.

Aidan P Maartens, Jutta Wellmann, Emma Wictome, Benjamin Klapholz, Hannah Green, Nicholas H Brown

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. The mechanical response of vinculin.Science advances · 2025
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  10. Epithelial morphogenesis in theFrontiers in cell and developmental biology · 2022
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  13. 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

6 authors at 1 institution in 1 country.

Aidan P MaartensDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK.
Jutta WellmannDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK.
Emma WictomeDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK.
Benjamin KlapholzDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK.
Hannah GreenDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK.
Nicholas H BrownDepartment of Physiology, Development and Neuroscience, and the Gurdon Institute, University of Cambridge, Downing St., Cambridge CB2 1DY, UK nb117@cam.ac.uk.ORCID 0000-0002-8958-7017
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D526102/1Biotechnology and Biological Sciences Research Council BB/L006669/1Cancer Research UK C6946/A14492Wellcome Trust 086451Wellcome Trust 092096
6 · The paper itself

Abstract

Vinculin is a highly conserved protein involved in cell adhesion and mechanotransduction, and both gain and loss of its activity causes defective cell behaviour. Here, we examine how altering vinculin activity perturbs integrin function within the context of Drosophila development. Whereas loss of vinculin produced relatively minor phenotypes, gain of vinculin activity, through a loss of head-tail autoinhibition, caused lethality. The minimal domain capable of inducing lethality is the talin-binding D1 domain, and this appears to require talin-binding activity, as lethality was suppressed by competition with single vinculin-binding sites from talin. Activated Drosophila vinculin triggered the formation of cytoplasmic adhesion complexes through the rod of talin, but independently of integrin. These complexes contain a subset of adhesion proteins but no longer link the membrane to actin. The negative effects of hyperactive vinculin were segregated into morphogenetic defects caused by its whole head domain and lethality caused by its D1 domain. These findings demonstrate the crucial importance of the tight control of the activity of vinculin.

Indexed as

AnimalsCell AdhesionCytoplasmDrosophila melanogasterEmbryo, NonmammalianIntegrinsModels, BiologicalMusclesProtein AggregatesProtein BindingProtein DomainsVinculinIntegrinsProtein AggregatesVinculinAdhesionDrosophilaIntegrinProtein complexRheaTalinVinculin

Identifiers

PMID27737911
PMCPMC5201009
OpenAlexW2530842989

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.