Evidence map›Paper›PMID 35259013›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

ATP allosterically stabilizes integrin-linked kinase for efficient force generation.

Isabel M Martin, Michele M Nava, Sara A Wickström, Frauke Gräter

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 34% 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

11 citing papers in PubMed, 9 citations in OpenAlex.

  1. Differential Transcriptomic and Adhesion Responses of Human Periodontal Ligament Cells to Cyclic and Static Hydrostatic Pressure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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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

4 authors at 3 institutions in 2 countries.

Isabel M MartinMolecular Biomechanics, Heidelberg Institute for Theoretical Studies, 69118 Heidelberg, Germany.ORCID 0000-0002-8799-4671
Michele M NavaHelsinki Institute of Life Science, Biomedicum Helsinki, University of Helsinki, 00290 Helsinki, Finland.ORCID 0000-0001-8733-6364
Sara A WickströmHelsinki Institute of Life Science, Biomedicum Helsinki, University of Helsinki, 00290 Helsinki, Finland.ORCID 0000-0001-6383-6292
Frauke GräterMolecular Biomechanics, Heidelberg Institute for Theoretical Studies, 69118 Heidelberg, Germany.ORCID 0000-0003-2891-3381
University of Helsinki · FIHeidelberg Institute for Theoretical Studies · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SignificanceThe pseudokinase integrin-linked kinase (ILK) is a central component of focal adhesions, cytoplasmic multiprotein complexes that integrate and transduce biochemical and mechanical signals from the extracellular environment into the cell and vice versa. However, the precise molecular functions, particularly the mechanosensory properties of ILK and the significance of retained adenosine triphosphate (ATP) binding, are still unclear. Combining molecular-dynamics simulations with cell biology, we establish a role for ATP binding to pseudokinases. We find that ATP promotes the structural stability of ILK, allosterically influences the interaction between ILK and its binding partner parvin at adhesions, and enhances the mechanoresistance of this complex. On the cellular level, ATP binding facilitates efficient traction force buildup, focal adhesion stabilization, and efficient cell migration.

Indexed as

ActomyosinAdenosine TriphosphateAllosteric RegulationBinding SitesCell AdhesionCell MovementEnzyme StabilityFocal AdhesionsMechanotransduction, CellularMicrofilament ProteinsModels, MolecularMolecular ConformationMutationProtein BindingProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesActomyosinAdenosine TriphosphateMicrofilament ProteinsProtein Serine-Threonine KinasesScaffold Protein ILKfocal adhesionintegrin-linked kinasemolecular dynamicstraction force microscopy

Identifiers

PMID35259013
PMCPMC8933812
OpenAlexW4220913757

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.