Evidence map›Paper›PMID 30254023›Full record

ArticleJournal of cell science2018

Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading.

Yasmin A Kadry, Clotilde Huet-Calderwood, Bertrand Simon, David A Calderwood

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2018. 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
3.3field-weighted citation impact, top 8% 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, 32 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
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. ATP allosterically stabilizes integrin-linked kinase for efficient force generation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Integrin-linked kinase (ILK): the known vs. the unknown and perspectives.Cellular and molecular life sciences : CMLS · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021
    Review
  16. Article
  17. Article
  18. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  19. Article
  20. Article
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 1 institution in 1 country.

Yasmin A KadryFrom the Department of Pharmacology, Yale University, New Haven CT 06510, USA.ORCID 0000-0002-4209-7416
Clotilde Huet-CalderwoodFrom the Department of Pharmacology, Yale University, New Haven CT 06510, USA.
Bertrand SimonFrom the Department of Pharmacology, Yale University, New Haven CT 06510, USA.ORCID 0000-0002-1825-053X
David A CalderwoodFrom the Department of Pharmacology, Yale University, New Haven CT 06510, USA david.calderwood@yale.edu.ORCID 0000-0002-0791-4142
Yale University · US

Funding

Translational CoreP01DK057751 · NIDDK · YALE UNIVERSITY · PI NATHANSON, MICHAEL H · 2001 to 2020
$25.6M
INSTITUTIONAL NATIONAL RESEARCH SERVICE AWARDT32GM007324 · NIGMS · YALE UNIVERSITY · PI BENNETT, ANTON M · 1987 to 2022
$6.2M
Integrin-Filamin Interactions in Migration and SignalingR01GM068600 · NIGMS · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2003 to 2016
$4.4M
Molecular assembly and regulation of the cerebral cavernous malformation complexR01NS085078 · NINDS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2013 to 2017
$1.8M
NIDDK NIH HHS P01 DK057751NIGMS NIH HHS R01 GM068600NIGMS NIH HHS T32 GM007324NINDS NIH HHS R01 NS085078
6 · The paper itself

Abstract

The integrin-associated adaptor proteins integrin-linked kinase (ILK) and kindlin-2 play central roles in integrin signaling and control of cell morphology. A direct ILK-kindlin-2 interaction is conserved across species and involves the F2PH subdomain of kindlin-2 and the pseudokinase domain (pKD) of ILK. However, complete understanding of the ILK-kindlin-2 interaction and its role in integrin-mediated signaling has been impeded by difficulties identifying the binding site for kindlin-2 on ILK. We used conservation-guided mapping to dissect the interaction between ILK and kindlin-2 and identified a previously unknown binding site for kindlin-2 on the C-lobe of the pKD of ILK. Mutations at this site inhibit binding to kindlin-2 while maintaining structural integrity of the pKD. Importantly, kindlin-binding-defective ILK mutants exhibit impaired focal adhesion localization and fail to fully rescue the spreading defects seen in ILK knockdown cells. Furthermore, kindlin-2 mutants with impaired ILK binding are also unable to fully support cell spreading. Thus, the interaction between ILK and kindlin-2 is critical for cell spreading and focal adhesion localization, representing a key signaling axis downstream of integrins.This article has an associated First Person interview with the first author of the paper.

Indexed as

Amino Acid SequenceCell AdhesionFocal AdhesionsHumansMembrane ProteinsNeoplasm ProteinsProtein Serine-Threonine KinasesScaffold Protein ILKSignal TransductionFERMT3 protein, humanMembrane ProteinsNeoplasm ProteinsProtein Serine-Threonine KinasesScaffold Protein ILKIntegrinIntegrin-linked kinaseKindlin-2

Identifiers

PMID30254023
PMCPMC6215391
OpenAlexW2894197700

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.