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Force interacts with macromolecular structure in activation of TGF-β
Open accessAbstract
Integrins are adhesion receptors that transmit force across the plasma membrane between extracellular ligands and the actin cytoskeleton. In activation of the transforming growth factor-β1 precursor (pro-TGF-β1), integrins bind to the prodomain, apply force, and release the TGF-β growth factor. However, we know little about how integrins bind macromolecular ligands in the extracellular matrix or transmit force to them. Here we show how integrin α V β 6 binds pro-TGF-β1 in an orientation biologically relevant for force-dependent release of TGF-β from latency. The conformation of the prodomain integrin-binding motif differs in the presence and absence of integrin binding; differences extend well outside the interface and illustrate how integrins can remodel extracellular matrix. Remodelled residues outside the interface stabilize the integrin-bound conformation, adopt a conformation similar to earlier-evolving family members, and show how macromolecular components outside the binding motif contribute to integrin recognition. Regions in and outside the highly interdigitated interface stabilize a specific integrin/pro-TGF-β orientation that defines the pathway through these macromolecules which actin-cytoskeleton-generated tensile force takes when applied through the integrin β-subunit. Simulations of force-dependent activation of TGF-β demonstrate evolutionary specializations for force application through the TGF-β prodomain and through the β- and not α-subunit of the integrin.
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“mice genetically engineered to replace murine β8 with its human ortholog demonstrated that a blocking antibody against human αvβ8 blocks TGF-β1 activation and protects against allergic airway inflammation and remodeling induced by cigarette smoke106”
From Fibrosis: from mechanisms to medicines (2020) · cites this paper as [106]
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Atypical interactions of integrin α V β 8 with pro-TGF-β1
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Self-citationFrom a Helix to a Small Cycle: Metadynamics‐Inspired αvβ6 Integrin Selective Ligands
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Low-affinity integrin states have faster ligand-binding kinetics than the high-affinity state
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Self-citationGeneral structural features that regulate integrin affinity revealed by atypical αVβ8
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Metadata
- Authors
- Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A.
- Affiliations
- Boston Children's Hospital (US)
- Northeastern University (US)
- Corresponding author
- Springer, Timothy A.
- ORCID
- Venue
- Nature
- Published
- 2017-01-25
- Volume
- 542
- Issue
- 7639
- Pages
- 55-59
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5586147
- OpenAlex
- W2582355481
- Cited by
- 273
- References
- 30
- Citations by year
- 2026: 13 · 2025: 34 · 2024: 30 · 2023: 24 · 2022: 28 · 2021: 37 · 2020: 34 · 2019: 21 · 2018: 27 · 2017: 23
- FWCI
- 23.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Charles A. King Trust
- National Institutes of Health
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR067288)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- TGF-beta activation, integrin αvβ6, latent TGF-beta, integrin binding, co-crystal structure, extracellular matrix remodeling, integrin beta subunit, conformational change
- MeSH terms
- Amino Acid Sequence, Antigens, Neoplasm, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Conformation, Integrins, Crystallography, X-Ray, Evolution, Molecular, Transforming Growth Factor beta1
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