ArticleeLife2016
Implications of the differing roles of the β1 and β3 transmembrane and cytoplasmic domains for integrin function.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- FCHo2, not talin, enables inside-out activation of integrin ɑvβ5 in curved adhesions.Nature communications · 2026Article
- FCHo2, instead of talin, enables inside-out activation of integrin ɑvβ5 in curved adhesions.bioRxiv : the preprint server for biology · 2025Article
- Integrating integrins with the hallmarks of cancer.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
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- From mesenchymal niches to engineeredMaterials today. Bio · 2022Article
- Rac1 promotes kidney collecting duct integrity by limiting actomyosin activity.The Journal of cell biology · 2021Article
- The Vanderbilt O'Brien Kidney Center.American journal of physiology. Renal physiology · 2021Review
- The progression of intracerebral hemorrhage (ICH) is related to the expression of integrin Β1 (ITGB1).Chinese neurosurgical journal · 2021Article
- Integrin Binding Dynamics Modulate Ligand-Specific Mechanosensing in Mammary Gland Fibroblasts.iScience · 2020Article
- Frontline Science: A flexible kink in the transmembrane domain impairs β2 integrin extension and cell arrest from rolling.Journal of leukocyte biology · 2020Article
- MiR-148a inhibits the proliferation and migration of glioblastoma by targeting ITGA9.Human cell · 2019Article
- Unique transmembrane domain interactions differentially modulate integrin αvβ3 and αIIbβ3 function.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Multiscale model of integrin adhesion assembly.PLoS computational biology · 2019Article
- Intramembrane ionic protein-lipid interaction regulates integrin structure and function.PLoS biology · 2018Article
- De novo designed transmembrane peptides activating the α5β1 integrin.Protein engineering, design & selection : PEDS · 2018Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- Transmission of integrin β7 transmembrane domain topology enables gut lymphoid tissue development.The Journal of cell biology · 2018Article
- Talin regulates integrin β1-dependent and -independent cell functions in ureteric bud development.Development (Cambridge, England) · 2017Article
- Lucky kindlin: A cloverleaf at the integrin tail.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Integrins are transmembrane receptors composed of α and β subunits. Although most integrins contain β1, canonical activation mechanisms are based on studies of the platelet integrin, αIIbβ3. Its inactive conformation is characterized by the association of the αIIb transmembrane and cytosolic domain (TM/CT) with a tilted β3 TM/CT that leads to activation when disrupted. We show significant structural differences between β1 and β3 TM/CT in bicelles. Moreover, the 'snorkeling' lysine at the TM/CT interface of β subunits, previously proposed to regulate αIIbβ3 activation by ion pairing with nearby lipids, plays opposite roles in β1 and β3 integrin function and in neither case is responsible for TM tilt. A range of affinities from almost no interaction to the relatively high avidity that characterizes αIIbβ3 is seen between various α subunits and β1 TM/CTs. The αIIbβ3-based canonical model for the roles of the TM/CT in integrin activation and function clearly does not extend to all mammalian integrins.
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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.