ArticleThe Journal of biological chemistry2022
Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- The potential and therapeutic advances of the integrin family in neurological disorders.Neural regeneration research · 2026Article
- DynMoCo: A novel AI framework to reveal modular substructures of protein from molecular dynamics.Biophysical journal · 2026Article
- Integrin α7-Driven Senescence-Associated Follicular Helper T Cell Adhesion Induces Tertiary Lymphoid Structures in Nishiura Mice.International journal of molecular sciences · 2026Article
- Cellular crosstalk and signaling networks in the rheumatoid arthritis synovial microenvironment.Journal of translational medicine · 2026Review
- Structural basis for the differential recognition of integrin αvβ3 by rhodostomin and trimucrin.Communications biology · 2026Article
- DynMoCo: a Novel AI Framework to Reveal Modular Substructures of Protein From Molecular Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Article
- Insulin-like growth factor 1 receptor regulates breast cancer cell adhesion through beta-1 integrin.Frontiers in endocrinology · 2026Article
- Rapid estimation of protein folding pathways from sequence alone using AlphaFold2.Nature communications · 2025Article
- Insulin-Like Growth Factor 1 Receptor Regulates Breast Cancer Cell Adhesion through Beta-1 Integrin.bioRxiv : the preprint server for biology · 2025Article
- Exploring the mechanism of fibronectin extra domain B in the tumor microenvironment and implications for targeted immunotherapy and diagnostics (Review).Molecular medicine reports · 2025Review
- Isogenic Transplantation of Hybrid Artificial Pleural Tissue Consisting of Rat Cells and Polyglycolic Acid Nanofiber Sheet Induces Restoration of Mesothelial Defects in Rat Model.Artificial organs · 2025Article
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- Role and mechanism of Integrin α5β1 in bone formation and disease.Frontiers in cell and developmental biology · 2025Review
- The Complex Role of Matrix Metalloproteinase-2 (MMP-2) in Health and Disease.International journal of molecular sciences · 2024Review
- AlphaFold2bioRxiv : the preprint server for biology · 2024Article
- Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024Article
- Signaling Pathways of the Insulin-like Growth Factor Binding Proteins.Endocrine reviews · 2023Article
- The Role of Integrins for Mediating Nanodrugs to Improve Performance in Tumor Diagnosis and Treatment.Nanomaterials (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Integrin α5β1 mediates cell adhesion to the extracellular matrix by binding fibronectin (Fn). Selectivity for Fn by α5β1 is achieved through recognition of an RGD motif in the 10th type III Fn domain (Fn10) and the synergy site in the ninth type III Fn domain (Fn9). However, details of the interaction dynamics are unknown. Here, we compared synergy-site and Fn-truncation mutations for their α5β1-binding affinities and stabilities. We also interrogated binding of the α5β1 ectodomain headpiece fragment to Fn using hydrogen-deuterium exchange (HDX) mass spectrometry to probe binding sites and sites of integrin conformational change. Our results suggest the synergistic effect of Fn9 requires both specific residues and a folded domain. We found some residues considered important for synergy are required for stability. Additionally, we show decreases in fibronectin HDX are localized to a synergy peptide containing contacting residues in two β-strands, an intervening loop in Fn9, and the RGD-containing loop in Fn10, indicative of binding sites. We also identified binding sites in the α5-subunit β-propeller domain for the Fn9 synergy site and in the β1-subunit βI domain for Fn10 based on decreases in α5β1 HDX. Interestingly, the dominant effect of Fn binding was an increase in α5β1 deuterium exchange distributed over multiple sites that undergo changes in conformation or solvent accessibility and appear to be sites where energy is stored in the higher-energy, open-integrin conformation. Together, our results highlight regions important for α5β1 binding to Fn and dynamics associated with this interaction.
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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.