ArticleThe Journal of biological chemistry2016
Molecular Basis of the Ligand Binding Specificity of αvβ8 Integrin.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Targeting α v β 8 Integrin with mAb MEDI8367 Prevents Fibrosis in Preclinical Models of CKD.Kidney360 · 2026Article
- Gene choice in cancer cells is exclusive in ion transport but concurrent in DNA replication.Computational and structural biotechnology journal · 2024Article
- The characteristics and the multiple functions of integrin β1 in human cancers.Journal of translational medicine · 2023Review
- CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023Review
- Neuropilin-1 and Integrins as Receptors for Chromogranin A-Derived Peptides.Pharmaceutics · 2022Review
- Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.Chemical reviews · 2022Review
- Molecular Signature of Astrocytes for Gene Delivery by the Synthetic Adeno-Associated Viral Vector rAAV9P1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- TGFβ: Signaling Blockade for Cancer Immunotherapy.Annual review of cancer biology · 2022Article
- The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.PLoS pathogens · 2021Article
- Pancreatic cancer cells render tumor-associated macrophages metabolically reprogrammed by a GARP and DNA methylation-mediated mechanism.Signal transduction and targeted therapy · 2021Article
- Regulatory T cells promote innate inflammation after skin barrier breach via TGF-β activation.Science immunology · 2021Article
- A tumor-specific mechanism of TScience immunology · 2021Article
- The right ventricular transcriptome signature in Ossabaw swine with cardiometabolic heart failure: implications for the coronary vasculature.Physiological genomics · 2021Article
- Discovery of a new class of integrin antibodies for fibrosis.Scientific reports · 2021Article
- αvβ8 integrin adhesion and signaling pathways in development, physiology and disease.Journal of cell science · 2020Review
- Article
- Laminin is the ECM niche for trophoblast stem cells.Life science alliance · 2020Article
- Integrin αvβ8 serves as a Novel Marker of Poor Prognosis in Colon Carcinoma and Regulates Cell Invasiveness through the Activation of TGF-β1.Journal of Cancer · 2020Article
- Integrin αvβ8-expressing tumor cells evade host immunity by regulating TGF-β activation in immune cells.JCI insight · 2018Article
- Laminin γ1 C-terminal Glu to Gln mutation induces early postimplantation lethality.Life science alliance · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
αvβ8 is an integrin that recognizes an Arg-Gly-Asp (RGD) motif and interacts with fibronectin, vitronectin, and latent TGF-β1. We comprehensively determined the binding activity of the αvβ8 integrin toward 25 secreted proteins having an RGD motif. The αvβ8 integrin strongly bound to latent TGF-β1 but showed marginal activity for other RGD-containing proteins, including fibronectin and vitronectin. Site-directed mutagenesis of latent TGF-β1 demonstrated that the high affinity binding of αvβ8 integrin to latent TGF-β1 was defined by Leu-218 immediately following the RGD motif within the latency-associated peptide of TGF-β1. Consistent with the critical role of Leu-218 in latent TGF-β1 recognition by αvβ8 integrin, a 9-mer synthetic peptide containing an RGDL sequence strongly inhibited interactions of latent TGF-β1 with αvβ8 integrin, whereas a 9-mer peptide with an RGDA sequence was ∼60-fold less inhibitory. Because αvβ3 integrin did not exhibit strong binding to latent TGF-β1 or distinguish between RGDL- and RGDA-containing peptides, we explored the mechanism by which the integrin β8 subunit defines the high affinity binding of latent TGF-β1 by αvβ8 integrin. Production of a series of swap mutants of integrin β8 and β3 subunits indicated that the high affinity binding of αvβ8 integrin with latent TGF-β1 was ensured by interactions between the Leu-218 residue and the β8 I-like domain, with the former serving as an auxiliary recognition residue defining the restricted ligand specificity of αvβ8 integrin toward latent TGF-β1. In support of this conclusion, high affinity binding toward the αvβ8 integrin was conferred on fibronectin by substitution of its RGDS motif with an RGDL sequence.
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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.