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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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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Barlowe, C. K. (1994) · Cell · doi:10.1016/0092-8674(94)90138-4 · Cited by 1,329
Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 1,011
BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
Lee, M. C. S., Miller, E. A., Goldberg, J., Orci, L., & Schekman, R. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.105307 · Cited by 813
Self-citationMatsuoka, K., Orci, L., AMHERDT, M., Bednarek, S. Y., Hamamoto, S., Schekman, R. W., & Yeung, T. (1998) · Cell · doi:10.1016/s0092-8674(00)81577-9 · Cited by 631
Tau protein binds to microtubules through a flexible array of distributed weak sites.
Butner, K. A., & Kirschner, M. W. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.3.717 · Cited by 550
Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat
Bi, X., Corpina, R. A., & Goldberg, J. M. (2002) · Nature · doi:10.1038/nature01040 · Cited by 474
Self-citationThe organization of endoplasmic reticulum export complexes.
Bannykh, S. I., Rowe, T., & Balch, W. E. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.1.19 · Cited by 440
TANGO1 Facilitates Cargo Loading at Endoplasmic Reticulum Exit Sites
Saito, K., Chen, M., Bard, F., Chen, S., Zhou, H., Woodley, D. T., Polischuk, R., Schekman, R. W., & Malhotra, V. (2009) · Cell · doi:10.1016/j.cell.2008.12.025 · Cited by 387
Structure of the Sec13/31 COPII coat cage
Stagg, S. M., Gürkan, C., Fowler, D. M., LaPointe, P., Foss, T. R., Potter, C. S., Carragher, B. O., & Balch, W. E. (2006) · Nature · doi:10.1038/nature04339 · Cited by 334
Ubiquitin-dependent regulation of COPII coat size and function
Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Baumgärtel, C., Schekman, R., & Rape, M. (2012) · Nature · doi:10.1038/nature10822 · Cited by 330
Boyadjiev, S. A., Fromme, J. C., Ben, J., Chong, S. S., Nauta, C., Hur, D. J., Zhang, G., Hamamoto, S., Schekman, R. W., Ravazzola, M., et al. (2006) · Nature Genetics · doi:10.1038/ng1876 · Cited by 314
Bi, X., Mancias, J. D., & Goldberg, J. D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.10.006 · Cited by 231
Self-citationStructural basis of cargo membrane protein discrimination by the human COPII coat machinery
Mancias, J. D., & Goldberg, J. D. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.208 · Cited by 216
Self-citationGlobal defects in collagen secretion in a Mia3/TANGO1 knockout mouse
Wilson, D. G., Phamluong, K., Li, L., Sun, M., Cao, T. C., Liu, P. S., Modrusan, Z. D., Sandoval, W. N., Rangell, L. K., Carano, R. A. D., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007162 · Cited by 202
Zeuschner, D., Geerts, W. J. C., van Donselaar, E. G., Humbel, B. M., Slot, J. W., Koster, A. J., & Klumperman, J. (2006) · Nature Cell Biology · doi:10.1038/ncb1371 · Cited by 193
GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes
Futai, E., Hamamoto, S., Orci, L., & Schekman, R. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600428 · Cited by 184
Saito, K., Yamashiro, K., Ichikawa, Y., Erlmann, P., Kontani, K., Malhotra, V., & Katada, T. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0143 · Cited by 176
Townley, A. K., Feng, Y., Schmidt, K., Carter, D. A., Porter, R., Verkade, P., & Stephens, D. J. (2008) · Journal of Cell Science · doi:10.1242/jcs.031070 · Cited by 174
Garbes, L., Kim, K., Rieß, A., Hoyer-Kuhn, H., Beleggia, F., Bevot, A., Kim, M. J., Huh, Y. H., Kweon, H.-S., Savarirayan, R., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.01.002 · Cited by 173
Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle
Venditti, R., Scanu, T., Santoro, M. C., Tullio, G. D., Spaar, A., Gaibisso, R., Beznoussenko, G. V., Aa, M., Aa, M., Zelante, L., et al. (2012) · Science · doi:10.1126/science.1224947 · Cited by 165
Converging on proline: the mechanism of WW domain peptide recognition.
Zarrinpar, A., & Lim, W. A. (2000) · Nature Structural Biology · doi:10.1038/77891 · Cited by 153
Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis
Sato, K., & Nakano, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb893 · Cited by 146
The structure of the COPII transport-vesicle coat assembled on membranes
Zanetti, G., Prinz, S., Daum, S., Meister, A., Schekman, R. W., Bacia, K., & Briggs, J. A. G. (2013) · eLife · doi:10.7554/elife.00951 · Cited by 131
TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export
Santos, A. J. M., Raote, I., Scarpa, M., Brouwers, N., & Malhotra, V. (2015) · eLife · doi:10.7554/elife.10982 · Cited by 113
ER-to-Golgi transport: Form and formation of vesicular and tubular carriers
Watson, P., & Stephens, D. J. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.03.003 · Cited by 101
Multibudded tubules formed by COPII on artificial liposomes
Bacia, K., Futai, E., Prinz, S., Meister, A., Daum, S., Glatte, D., Briggs, J. A. G., & Schekman, R. W. (2011) · Scientific Reports · doi:10.1038/srep00017 · Cited by 89
Nogueira, C., Erlmann, P., Villeneuve, J., Santos, A. J. M., Martínez‐Alonso, E., Martínez‐Menárguez, J. A., & Malhotra, V. (2014) · eLife · doi:10.7554/elife.02784 · Cited by 83
A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry
Noble, A. J., Zhang, Q., O’Donnell, J., Hariri, H. H., Bhattacharya, N., Marshall, A. G., & Stagg, S. M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2467 · Cited by 61
Diversity of polyproline recognition by EVH1 domains
Francis, C. P. (2009) · Frontiers in bioscience · doi:10.2741/3281 · Cited by 48
Helm, J. R., Bentley, M., Thorsen, K. D., Wang, T., Foltz, L., Oorschot, V. M. J., Klumperman, J., & Hay, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561829 · Cited by 46
ALG-2 Attenuates COPII Budding In Vitro and Stabilizes the Sec23/Sec31A Complex
la Cour, J. M., Schindler, A. J., Berchtold, M. W., & Schekman, R. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075309 · Cited by 46
Takahashi, T., Kojima, K., Zhang, W., Sasaki, K. E., Ito, M., SUZUKI, H., Kawasaki, M., Soichi Wakatsuki, A., Takahara, T., Shibata, H., et al. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16023677 · Cited by 33
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Computed structures of core eukaryotic protein complexes
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Gómez‐Navarro, N., & Miller, E. A. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201610031 · Cited by 276
ESCRT-dependent cargo sorting at multivesicular endosomes
Frankel, E. B., & Audhya, A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.08.020 · Cited by 178
Raote, I., Bellido, M., Santos, A. J. M., Foresti, O., Zhang, C., Parajo, M. F. G., Campelo, F., & Malhotra, V. (2018) · eLife · doi:10.7554/elife.32723 · Cited by 163
Deniger, D. C., Pasetto, A., Robbins, P. F., Gartner, J. J., Prickett, T. D., Paria, B. C., Malekzadeh, P., Jia, L., Yossef, R., Langhan, M. M., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-0573 · Cited by 157
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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