ArticleJournal of cell science2014
Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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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.
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Who cites it
41 citing papers in PubMed, 62 citations in OpenAlex.
- 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 · 2026Article
- The ILK-PINCH-parvin complex: a conserved primary adhesome regulating biological processes.Histochemistry and cell biology · 2025Review
- Hydrophobicity-Driven Disruption Mechanism in Kindlin-3 Induced by Leukocyte Adhesion Deficiency Mutation.ACS omega · 2025Article
- β-arrestin 1 and integrin-linked kinase interact in epidermal keratinocytes and regulate cell motility.Tissue barriers · 2025Article
- Structure, signal transduction, activation, and inhibition of integrin αIIbβ3.Thrombosis journal · 2023Review
- Genetic analysis suggests a surface of PAT-4 (ILK) that interacts with UNC-112 (kindlin).G3 (Bethesda, Md.) · 2022Article
- Review
- Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022Review
- Kindlin-2 Promotes Chondrogenesis and Ameliorates IL-1beta-Induced Inflammation in Chondrocytes Cocultured with BMSCs in the Direct Contact Coculture System.Oxidative medicine and cellular longevity · 2022Article
- Examination of FERMT1 expression in placental chorionic villi and its role in HTR8-SVneo cell invasion.Histochemistry and cell biology · 2021Article
- Molecular motion and tridimensional nanoscale localization of kindlin control integrin activation in focal adhesions.Nature communications · 2021Article
- Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021Review
- Kindlin-3 mutation in mesenchymal stem cells results in enhanced chondrogenesis.Experimental cell research · 2021Article
- Missense mutation of a conserved residue in UNC-112 (kindlin) eliminates binding to PAT-4 (ILK).microPublication biology · 2021Article
- PINCH-1 regulates mitochondrial dynamics to promote proline synthesis and tumor growth.Nature communications · 2020Article
- Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding.The Journal of biological chemistry · 2020Article
- Structure basis of the FERM domain of kindlin-3 in supporting integrin αIIbβ3 activation in platelets.Blood advances · 2020Article
- Structural basis of human full-length kindlin-3 homotrimer in an auto-inhibited state.PLoS biology · 2020Article
- Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020Review
- Macrophage Migration and Phagocytosis Are Controlled by Kindlin-3's Link to the Cytoskeleton.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
Kindlins are essential FERM-domain-containing focal adhesion (FA) proteins required for proper integrin activation and signaling. Despite the widely accepted importance of each of the three mammalian kindlins in cell adhesion, the molecular basis for their function has yet to be fully elucidated, and the functional differences between isoforms have generally not been examined. Here, we report functional differences between kindlin-2 and -3 (also known as FERMT2 and FERMT3, respectively); GFP-tagged kindlin-2 localizes to FAs whereas kindlin-3 does not, and kindlin-2, but not kindlin-3, can rescue α5β1 integrin activation defects in kindlin-2-knockdown fibroblasts. Using chimeric kindlins, we show that the relatively uncharacterized kindlin-2 F2 subdomain drives FA targeting and integrin activation. We find that the integrin-linked kinase (ILK)-PINCH-parvin complex binds strongly to the kindlin-2 F2 subdomain but poorly to that of kindlin-3. Using a point-mutated kindlin-2, we establish that efficient kindlin-2-mediated integrin activation and FA targeting require binding to the ILK complex. Thus, ILK-complex binding is crucial for normal kindlin-2 function and differential ILK binding contributes to kindlin isoform specificity.
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Registered trials
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.