ArticleCell adhesion & migration
Structural basis of transmembrane domain interactions in integrin signaling.
Article in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed.
- ITGA2B/ITGB3-Related Macrothrombocytopenia Associated With Gain-of-Function Mutations in ITGA2B or ITGB3 Genes.Journal of cellular and molecular medicine · 2026Review
- Impact of Lipid Bilayer Composition and Physicochemical Properties on Constitution of a Transmembrane Helical Peptide into Exosome-Mimetic Vesicles.Molecular pharmaceutics · 2025Article
- Twins With an Identical Novel Mutation inAnnals of laboratory medicine · 2024Article
- αIIbβ3 variants in ten families with autosomal dominant macrothrombocytopenia: Expanding the mutational and clinical spectrum.PloS one · 2020Article
- Integrins as Therapeutic Targets: Successes and Cancers.Cancers · 2017Review
- Inhibition of PlexA1-mediated brain tumor growth and tumor-associated angiogenesis using a transmembrane domain targeting peptide.Oncotarget · 2016Article
- Annular anionic lipids stabilize the integrin αIIbβ3 transmembrane complex.The Journal of biological chemistry · 2015Article
- Demonstration of novel gain-of-function mutations of αIIbβ3: association with macrothrombocytopenia and glanzmann thrombasthenia-like phenotype.Molecular genetics & genomic medicine · 2013Article
- Article
- The tail of integrin activation.Trends in biochemical sciences · 2011Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Cell surface receptors of the integrin family are pivotal to cell adhesion and migration. The activation state of heterodimeric alphabeta integrins is correlated to the association state of the single-pass alpha and beta transmembrane domains. The association of integrin alphaIIbbeta3 transmembrane domains, resulting in an inactive receptor, is characterized by the asymmetric arrangement of a straight (alphaIIb) and tilted (beta3) helix relative to the membrane in congruence to the dissociated structures. This allows for a continuous association interface centered on helix-helix glycine-packing and an unusual alphaIIb(GFF) structural motif that packs the conserved Phe-Phe residues against the beta3 transmembrane helix, enabling alphaIIb(D723)beta3(R995) electrostatic interactions. The transmembrane complex is further stabilized by the inactive ectodomain, thereby coupling its association state to the ectodomain conformation. In combination with recently determined structures of an inactive integrin ectodomain and an activating talin/beta complex that overlap with the alphabeta transmembrane complex, a comprehensive picture of integrin bi-directional transmembrane signaling has emerged.
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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.