The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats
Open accessAbstract
Significance: Proteins destined for secretion from cells enter the secretory pathway in coat protein complex II (COPII)-coated vesicles budding from the endoplasmic reticulum (ER). Most cargo proteins are small and exit the ER in 60-nm vesicles. However, some secretory cargos are too large to enter such carriers; in particular, the procollagen precursor of the extracellular matrix exits the ER as a 300- to 400-nm fibril. Recent research suggests that procollagen may be packaged into large COPII-coated tubules, guided by the receptor molecule TANGO1/cTAGE5. We show that each TANGO1/cTAGE5 receptor protein has a multiplicity of binding sites to recruit and concentrate COPII proteins. We propose the model that TANGO1/cTAGE5 instructs the COPII coat to form large tubular carriers.
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“Our model of the Sec23–Grh1 complex contains an interface between the Sec23 gelsolin domain and the PPP motif of Grh1 (80), and an interface between the Grh1 IDR and Sec23 involving a disorder-to-helical transition (fig. S25C).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [80]
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BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
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Bone Involvement in the Ehlers-Danlos Syndromes
Malfait, F., Syx, D., & Ishikawa, Y. (2024) · Biology of extracellular matrix · doi:10.1007/978-3-031-70835-0_3
New Trick for the Old COP: Cellular Physiology of COPII Condensation in Lipoprotein Secretion
Wang, X., Yang, K. L., & Chen, X.-W. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.70061
Ali, Y. T., Ravindran, A., Eichelmann, L., Odenthal, N., & Aherrahrou, R. (2025) · IUBMB Life · doi:10.1002/iub.70076
Emerging Matritherapies in Lung Fibrosis and Cancer
Staab-Weijnitz, C. A., Kandhari, K., Herrera, J., Hansen, K., Redente, E. F., & Roman, J. (2026) · Biology of extracellular matrix · doi:10.1007/978-3-032-22618-1_6
Distinct roles for TANGO1S domains in maintaining ER–Golgi architecture
Lawrence, E. A., Hodgson, L. R., Mantell, J., Prada-Sanchez, M. E., Hammond, C. L., Stephens, D. J., & Stevenson, N. L. (2026) · Journal of Cell Science · doi:10.1242/jcs.265001
Guo, Y., Zheng, J., Liu, L., Li, S., Zhang, M., & Ge, L. (2026) · EMBO Reports · doi:10.1038/s44319-026-00908-z
Metadata
- Authors
- Ma, W., & Goldberg, J.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Goldberg, Jonathan
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2016-08-22
- Volume
- 113
- Issue
- 36
- Pages
- 10061-10066
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5018777
- OpenAlex
- W2517050669
- Cited by
- 108
- References
- 36
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 12 · 2023: 9 · 2022: 10 · 2021: 17 · 2020: 8 · 2019: 11 · 2018: 15 · 2017: 7 · 2016: 1
- FWCI
- 7.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Memorial Sloan-Kettering Cancer Center (CA008748, P30 CA008748)
- National Cancer Institute (P30CA008748)
- Argonne National Laboratory
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- TANGO1, Sec23, Sec31, Sar1, proline-rich region, ER exit sites, coated vesicles, protein-protein interaction
- MeSH terms
- Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Antigens, Neoplasm, Binding Sites, Endoplasmic Reticulum, Humans, Models, Molecular, Neoplasm Proteins, Procollagen, Protein Binding, Recombinant Proteins, Gene Expression, Crystallography, X-Ray, Monomeric GTP-Binding Proteins, Amino Acid Motifs, Protein Transport, COP-Coated Vesicles, Vesicular Transport Proteins, Aryl Hydrocarbon Receptor Nuclear Translocator, Protein Interaction Domains and Motifs
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