ArticleThe Journal of biological chemistry2012
Biophysical analysis of Kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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.
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Who cites it
29 citing papers in PubMed.
- Beyond Integrin Activation: Kindlin-3 as an Organiser of Immune Receptor Signalling.International journal of molecular sciences · 2026Review
- Integrin-mediated mechanotransduction in the tumor microenvironment: macrophage-centered signaling mechanisms and immune remodeling.Journal of translational medicine · 2026Review
- Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026Review
- Talin and kindlin use integrin tail allostery and direct binding to activate integrins.Nature structural & molecular biology · 2023Article
- Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Integrin Regulators in Neutrophils.Cells · 2022Review
- Review
- Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022Review
- Mechanism of integrin activation by talin and its cooperation with kindlin.Nature communications · 2022Article
- Filamin A in platelets: Bridging the (signaling) gap between the plasma membrane and the actin cytoskeleton.Frontiers in molecular biosciences · 2022Review
- Review
- 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
- Macrophage Migration and Phagocytosis Are Controlled by Kindlin-3's Link to the Cytoskeleton.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Costameres, dense plaques and podosomes: the cell matrix adhesions in cardiovascular mechanosensing.Journal of muscle research and cell motility · 2019Review
- Kindlin supports platelet integrin αIIbβ3 activation by interacting with paxillin.Journal of cell science · 2017Article
- The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation.The Journal of biological chemistry · 2017Article
- Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.The Biochemical journal · 2017Article
- Structural basis of blocking integrin activation and deactivation for anti-inflammation.Journal of biomedical science · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Kindlin-3, a 75-kDa protein, has been shown to be critical for hemostasis, immunity, and bone metabolism via its role in integrin activation. The Kindlin family is hallmarked by a FERM domain comprised of F1, F2, and F3 subdomains together with an N-terminal F0 domain and a pleckstrin homology domain inserted in the F2 domain. Recombinant Kindlin-3 was cloned, expressed, and purified, and its domain organization was studied by x-ray scattering and other techniques to reveal an extended conformation. This unusual elongated structure is similar to that found in the paralogue Talin head domain. Analytical ultracentrifugation experiments indicated that Kindlin-3 forms a ternary complex with the Talin and β-integrin cytoplasmic tails. NMR showed that Kindlin-3 specifically recognizes the membrane-distal tail NPXY motif in both the β(1A) and β(1D) isoforms, although the interaction is stronger with β(1A). An upstream Ser/Thr cluster in the tails also plays a critical role. Overall these data support current biological, clinical, and mutational data on Kindlin-3/β-tail binding and provide novel insights into the overall conformation and interactions of Kindlin-3.
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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.