The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Adhesion G protein-coupled receptors are activated by exposure of a cryptic tethered agonist
Open accessAbstract
Significance: Adhesion G protein-coupled receptors (GPCRs) regulate tissue development and cancer progression. Intact adhesion GPCRs are unique two-protomer receptors that undergo biosynthetic self-proteolyzation at a conserved site between the extracellular domain and the seven transmembrane (7TM) domain. We demonstrate the activation mechanism of adhesion GPCRs. The 7TM domain N-terminal stalk lies encrypted within the noncovalently bound extracellular domain. When the extracellular domain is dissociated, perhaps naturally by ligand action, the 7TM stalk is revealed. We demonstrate that the stalk acts as a tethered agonist of the 7TM to facilitate direct activation of heterotrimeric G proteins. Synthetic peptides comprising adhesion GPCR 7TM domain stalks are sufficient receptor agonists, raising the possibility for the development of adhesion GPCR synthetic peptide modulators.
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Heterogeneity of tethered agonist signaling in adhesion G protein-coupled receptors
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Metadata
- Authors
- Stoveken, H. M., Hajduczok, A. G., Xu, L., & Tall, G. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2015-04-27
- Volume
- 112
- Issue
- 19
- Pages
- 6194-6199
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2010441615
- Cited by
- 277
- References
- 26
- FWCI
- 8.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Stoveken, H. M., Hajduczok, A. G., Xu, L., & Tall, G. G. (2015). Adhesion G protein-coupled receptors are activated by exposure of a cryptic tethered agonist. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1421785112
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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