Evidence map›Paper›PMID 21444757›Full record

ArticleJournal of cell science2011

A central multifunctional role of integrin-linked kinase at muscle attachment sites.

Christos G Zervas, Eleni Psarra, Victoria Williams, Esther Solomon, Katerina M Vakaloglou, Nicholas H Brown

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. 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
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  6. Epithelial morphogenesis in theFrontiers in cell and developmental biology · 2022
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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 4 institutions in 2 countries.

Christos G ZervasBiomedical Research Foundation, Academy of Athens, Division of Genetics, Soranou Efessiou 4, 11527 Athens, Greece. czervas@bioacademy.gr
Eleni Psarra
Victoria Williams
Esther Solomon
Katerina M Vakaloglou
Nicholas H Brown
Biomedical Research Foundation of the Academy of Athens · GRUniversity of Cambridge · GBAcademy of Athens · GRWellcome/Cancer Research UK Gurdon Institute · GB

Funding

Wellcome Trust 64098
6 · The paper itself

Abstract

Integrin-linked kinase (ILK) is an essential component of a multiprotein complex that links actin to the plasma membrane. Here, we have used a genetic approach to examine the molecular interactions that are essential for the assembly of this ILK-containing complex at Drosophila muscle attachment sites (MASs). We show that, downstream of integrins, talin plays a decisive role in the recruitment of three proteins: ILK, PINCH and paxillin. The accumulation of ILK at MASs appears to follow an amplification mechanism, suggesting that numerous binding sites are generated by minimal levels of the upstream integrin and talin effectors. This property suggests that ILK functions as an essential hub in the assembly of its partner proteins at sites of integrin adhesion. We found that PINCH stability, and its subcellular localization at MASs, depends upon ILK function, but that ILK stability and localization is not dependent upon PINCH. An in vivo structure-function analysis of ILK demonstrated that each ILK domain has sufficient information for its independent recruitment at embryonic MASs, whereas at later developmental stages only the kinase domain was effectively recruited. Our data strengthen the view that the ILK complex is assembled sequentially at sites of integrin adhesion by employing multiple molecular interactions, which collectively stabilize the integrin-actin link.

Indexed as

AnimalsDrosophilaIntegrinsMusclesPaxillinProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryScaffold Protein ILKIntegrinsPaxillinProtein Serine-Threonine KinasesScaffold Protein ILK

Identifiers

PMID21444757
PMCPMC3065386
OpenAlexW2005310286

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.