ArticleThe Journal of biological chemistry2014
Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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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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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.
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Who cites it
40 citing papers in PubMed, 60 citations in OpenAlex.
- Beyond Integrin Activation: Kindlin-3 as an Organiser of Immune Receptor Signalling.International journal of molecular sciences · 2026Review
- Structural basis of kindlin-3 in leukocyte adhesion deficiency III.Journal of thrombosis and haemostasis : JTH · 2026Article
- 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
- Kindlins in the cardiovascular system: from development to pathogenesis.Frontiers in cardiovascular medicine · 2026Review
- Integrin-linked kinase (ILK) in hematologic malignancies: Bridging molecular mechanisms to therapeutic innovation.BioImpacts : BI · 2026Review
- β-arrestin 1 and integrin-linked kinase interact in epidermal keratinocytes and regulate cell motility.Tissue barriers · 2025Article
- Static and Dynamic: Evolving Biomaterial Mechanical Properties to Control Cellular Mechanotransduction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Genetic analysis suggests a surface of PAT-4 (ILK) that interacts with UNC-112 (kindlin).G3 (Bethesda, Md.) · 2022Article
- Bottom-up reconstitution of focal adhesion complexes.The FEBS journal · 2022Review
- Mechanism of integrin activation by talin and its cooperation with kindlin.Nature communications · 2022Article
- ATP allosterically stabilizes integrin-linked kinase for efficient force generation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021Review
- Article
- Implicating ILK in inflammation.Blood · 2020Article
- Mechanosensing dysregulation in the fibroblast: A hallmark of the aging heart.Ageing research reviews · 2020Review
- 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
- GIV•Kindlin Interaction Is Required for Kindlin-Mediated Integrin Recognition and Activation.iScience · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Integrin-linked kinase (ILK) is a distinct intracellular adaptor essential for integrin-mediated cell-extracellular matrix adhesion, cell spreading, and migration. Acting as a major docking platform in focal adhesions, ILK engages many proteins to dynamically link integrins with the cytoskeleton, but the underlying mechanism remains elusive. Here, we have characterized the interaction of ILK with kindlin-2, a key regulator for integrin bidirectional signaling. We show that human kindlin-2 binds to human ILK with high affinity. Using systematic mapping approaches, we have identified a major ILK binding site involving a 20-residue fragment (residues 339-358) in kindlin-2. NMR-based analysis reveals a helical conformation of this fragment that utilizes its leucine-rich surface to recognize the ILK pseudokinase domain in a mode that is distinct from another ILK pseudokinase domain binding protein, α-parvin. Structure-based mutational experiments further demonstrate that the kindlin-2 binding to ILK is crucial for the kindlin-2 localization to focal adhesions and cell spreading (integrin outside-in signaling) but dispensable for the kindlin-2-mediated integrin activation (integrin inside-out signaling). These data define a specific mode of the kindlin-2/ILK interaction with mechanistic implications as to how it spatiotemporally mediates integrin signaling and cell adhesion.
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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.