The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography
Open accessPublished version of a preprint
Abstract
We report here transport of full-length epidermal growth factor receptor (EGFR), Insulin Receptor, 7-pass transmembrane receptor Smoothened, and 13-pass Sodium-iodide symporter to extracellular vesicles (EVs) for structural and functional studies. Mass spectrometry confirmed the transported proteins are the most abundant in EV membranes, and the presence of many receptor-interacting proteins in EVs demonstrates their utility for characterizing membrane protein interactomes. Cryo-electron tomography of EGFR-containing EVs reveals that EGFR forms clusters in both the presence and absence of EGF with a ~3 nm gap between the inner membrane and cytoplasmic density. EGFR extracellular region (ECR) dimers do not form regular arrays in these clusters. Subtomogram averaging of the 150 kDa EGF-bound EGFR ECR dimer yielded a 15 Å map into which the crystal structure of the ligand-bound EGFR ECR dimer fits well. These findings refine our understanding of EGFR activation, clustering, and signaling and establish EVs as a versatile platform for structural and functional characterization of human membrane proteins in cell-derived membranes.
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Accurate structure prediction of biomolecular interactions with AlphaFold 3
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Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways
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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
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Metadata
- Authors
- Gonzalez-Magaldi, M., Gullapalli, A., Papoulas, O., Liu, C., Leung, A. Y.-H., Guo, L., Brilot, A. F., Marcotte, E. M., Ke, Z., & Leahy, D. J.
- Affiliations
- Department of Molecular Biosciences, The University of Texas at Austin
- The University of Texas at Austin (US)
- Corresponding author
- Ke, Zunlong
- Leahy, Daniel J.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2025-06-02
- Volume
- 122
- Issue
- 23
- Pages
- e2424678122-e2424678122
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC12167996
- OpenAlex
- W4410948342
- Cited by
- 17
- References
- 7
- Citations by year
- 2026: 11 · 2025: 6
- FWCI
- 5.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- Cancer Prevention and Research Institute of Texas (RR160023, RR230050)
- Wojcicki Foundation (LC029)
- HHS | NIH | National Institute of General Medical Sciences (R35GM122480)
- DOD | USA | AFC | CCDC | ARO | Life Sciences Division, Army Research Office (@911NF-12-1-0390)
- Welch Foundation (F-1515)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- epidermal growth factor receptor, extracellular vesicles, receptor clustering, EGF binding, membrane protein structure, EGFR activation, subtomogram averaging, insulin receptor, Smoothened, sodium iodide symporter
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