ArticleNature structural & molecular biology2015
Structural mechanism of integrin inactivation by filamin.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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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
51 citing papers in PubMed, 98 citations in OpenAlex.
- Mechanical Signaling From ECMs to Nuclear Envelopes in Cell Transitions and Fate Decisions: A Review and Perspective on Adhesion-Niche-Based Anti-EndMT and Anti-EMT.Annals of biomedical engineering · 2026Review
- The Integrin Receptors: From Discovery to Structure to Medicines.Immunological reviews · 2025Review
- Fine-tuning levels of filamins a and b as a specific mechanism sustaining Th2 lymphocyte functions.Nature communications · 2024Article
- Charting the importance of filamin A posttranslational modifications.The Biochemical journal · 2024Review
- A novel replication initiation region encoded in a widespread Acinetobacter plasmid lineage carrying a blaNDM-1 gene.PloS one · 2024Article
- PACSIN2 regulates platelet integrin β1 hemostatic function.Journal of thrombosis and haemostasis : JTH · 2023Article
- Cryo-EM structures of full-length integrin αIIbβ3 in native lipids.Nature communications · 2023Article
- Article
- A novel association between platelet filamin A and soluble N-ethylmaleimide sensitive factor attachment proteins regulates granule secretion.Research and practice in thrombosis and haemostasis · 2023Article
- Organization, dynamics and mechanoregulation of integrin-mediated cell-ECM adhesions.Nature reviews. Molecular cell biology · 2023Review
- Review
- Targeting integrin pathways: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2023Review
- A gain-of-function filamin A mutation in mouse platelets induces thrombus instability.Journal of thrombosis and haemostasis : JTH · 2022Article
- The structural basis of β2 integrin intra-cellular multi-protein complexes.Biophysical reviews · 2022Review
- New insights into regulation of αIIbβ3 integrin signaling by filamin A.Research and practice in thrombosis and haemostasis · 2022Article
- Filamin A in platelets: Bridging the (signaling) gap between the plasma membrane and the actin cytoskeleton.Frontiers in molecular biosciences · 2022Review
- Integrin-Mediated Tumorigenesis and Its Therapeutic Applications.Frontiers in oncology · 2022Review
- Myosin-X and talin modulate integrin activity at filopodia tips.Cell reports · 2021Article
- Review
- Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications.Science signaling · 2021Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Activation of heterodimeric (αβ) integrin is crucial for regulating cell adhesion. Binding of talin to the cytoplasmic face of integrin activates the receptor, but how integrin is maintained in a resting state to counterbalance its activation has remained obscure. Here, we report the structure of the cytoplasmic domain of human integrin αIIbβ3 bound to its inhibitor, the immunoglobin repeat 21 of filamin A (FLNa-Ig21). The structure reveals an unexpected ternary complex in which FLNa-Ig21 not only binds to the C terminus of the integrin β3 cytoplasmic tail (CT), as previously predicted, but also engages N-terminal helices of αIIb and β3 CTs to stabilize an inter-CT clasp that helps restrain the integrin in a resting state. Combined with functional data, the structure reveals a new mechanism of filamin-mediated retention of inactive integrin, suggesting a new framework for understanding regulation of integrin activation and 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.