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Ubiquitin-dependent regulation of COPII coat size and function
Open accessAbstract
Packaging of proteins from the endoplasmic reticulum into COPII vesicles is essential for secretion. In cells, most COPII vesicles are approximately 60-80 nm in diameter, yet some must increase their size to accommodate 300-400 nm procollagen fibres or chylomicrons. Impaired COPII function results in collagen deposition defects, cranio-lenticulo-sutural dysplasia, or chylomicron retention disease, but mechanisms to enlarge COPII coats have remained elusive. Here, we identified the ubiquitin ligase CUL3-KLHL12 as a regulator of COPII coat formation. CUL3-KLHL12 catalyses the monoubiquitylation of the COPII-component SEC31 and drives the assembly of large COPII coats. As a result, ubiquitylation by CUL3-KLHL12 is essential for collagen export, yet less important for the transport of small cargo. We conclude that monoubiquitylation controls the size and function of a vesicle coat.
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“it can also assemble with specific co-adaptors to monoubiquitylate the COPII component SEC31 for collagen trafficking 90,91,92”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [92]
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Cites
Metastasis: from dissemination to organ-specific colonization
Nguyen, D. X., Bos, P. D., & Massagué, J. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2622 · Cited by 2,716
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,643
Control of the Embryonic Stem Cell State
Young, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.01.032 · Cited by 1,246
Myocardial Infarction Genetics Consortium (2009) · Nature Genetics · doi:10.1038/ng.327 · Cited by 1,088
Cancer as an overhealing wound: an old hypothesis revisited
Schäfer, M., & Werner, S. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2455 · Cited by 974
Furukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 759
Latent Bone Metastasis in Breast Cancer Tied to Src-Dependent Survival Signals
Zhang, X. H.-F., Wang, Q., Gerald, W. L., Hudis, C. A., Norton, L., Smid, M., Foekens, J. A., & Massagué, J. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.05.017 · Cited by 670
Activation of Phosphoinositide 3-OH Kinase by the α6β4 Integrin Promotes Carcinoma Invasion
Shaw, L. M., Rabinovitz, I., Wang, H. H.-F., Toker, A., & Mercurio, A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80486-9 · Cited by 613
Stephens, L., Sutherland, A. E., Klimanskaya, I. V., Andrieux, A., Meneses, J., Pedersen, R. A., & Damsky, C. H. (1995) · Genes & Development · doi:10.1101/gad.9.15.1883 · Cited by 596
Xu, L., Yue, W., Reboul, J., Vaglio, P., Shin, T.-H., Vidal, M., Elledge, S. J., & Harper, J. W. (2003) · Nature · doi:10.1038/nature01985 · Cited by 500
Integrins: masters and slaves of endocytic transport
Caswell, P. T., Vadrevu, S., & Norman, J. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2799 · Cited by 460
The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase
Pintard, L., Willis, J. H., Willems, A. R., Johnson, J.-L., Srayko, M., Kurz, T., Luke-Glaser, S., Mains, P. E., Tyers, M., Bowerman, B. A., et al. (2003) · Nature · doi:10.1038/nature01959 · Cited by 434
Global Identification of Modular Cullin-RING Ligase Substrates
Emanuele, M. J., Elia, A. E. H., Xu, Q., Thoma, C. R., Izhar, L., Leng, Y., Guo, A., Chen, Y., Rush, A. J., Hsu, P. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.019 · Cited by 405
Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cellsPreprint
Singer, J. D., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.18.2375 · Cited by 404
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
Self-citationAngers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364
Transmembrane collagen receptors
Leitinger, B. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154013 · Cited by 354
BTB/POZ Domain Proteins Are Putative Substrate Adaptors for Cullin 3 Ubiquitin Ligases
Geyer, R. K., Wee, S., Anderson, S., Yates, J. R., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00341-1 · Cited by 342
Zhu, W., Cowie, A., Wasfy, G. W., Penn, L. Z., Leber, B. F., & Andrews, D. W. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00788.x · Cited by 327
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
Self-citationStructure and Organization of Coat Proteins in the COPII Cage
Fath, S., Mancias, J. D., Bi, X., & Goldberg, J. D. (2007) · Cell · doi:10.1016/j.cell.2007.05.036 · Cited by 304
Identification of a physiological E2 module for the human anaphase-promoting complex
Williamson, A. P., Wickliffe, K. E., Mellone, B. G., Song, L., Karpen, G. H., & Rapé, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907887106 · Cited by 290
Self-citationStructural Basis for Cargo Regulation of COPII Coat Assembly
Stagg, S. M., LaPointe, P., Razvi, A., Gürkan, C., Potter, C. S., Carragher, B. O., & Balch, W. E. (2008) · Cell · doi:10.1016/j.cell.2008.06.024 · Cited by 274
Chen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Ding, M., Peng, H. B., & Shao, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.004 · Cited by 270
COPII-mediated vesicle formation at a glance
Jensen, D., & Schekman, R. W. (2010) · Journal of Cell Science · doi:10.1242/jcs.069773 · Cited by 237
Self-citationSumara, I., Quadroni, M., Frei, C., Olma, M. H., Sumara, G., Ricci, R., & Peter, M. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.019 · Cited by 234
Global 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
The Genetic Basis of a Craniofacial Disease Provides Insight into COPII Coat Assembly
Fromme, J. C., Ravazzola, M., Hamamoto, S., Balwi, M. A. A., Eyaid, W., Boyadjiev, S. A., Cosson, P., Schekman, R. W., & Orci, L. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.10.005 · Cited by 190
Self-citationSecretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation
Lang, M. R., Lapierre, L. A., Frotscher, M., Goldenring, J. R., & Knapik, E. W. (2006) · Nature Genetics · doi:10.1038/ng1880 · Cited by 190
Cell-Cell and Cell-Extracellular Matrix Interactions Regulate Embryonic Stem Cell Differentiation
Chen, S. S., Fitzgerald, W., Zimmerberg, J. J., Kleinman, H. K., & Margolis, L. B. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0419 · Cited by 190
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
Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER
Hughes, H., Budnik, A., Schmidt, K., Palmer, K. J., Mantell, J., Noakes, C., Johnson, A., Carter, D. A., Verkade, P., Watson, P., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.044032 · Cited by 160
Sarmah, S., Barrallo‐Gimeno, A., Melville, D. B., Topczewski, J., Solnica‐Krezel, L., & Knapik, E. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010367 · Cited by 143
Stephens, D. J., & Pepperkok, R. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.6.1149 · Cited by 125
COPII-coated vesicles: flexible enough for large cargo?
Fromme, J. C., & Schekman, R. W. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.06.004 · Cited by 103
Self-citationGenetic Analyses of Integrin SignalingPreprint
Wickstrom, S. A., Radovanac, K., & Fassler, R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005116 · Cited by 95
Geddis, A. E., & Prockop, D. J. (1993) · Matrix · doi:10.1016/s0934-8832(11)80045-4 · Cited by 80
Identification of specific autoantigens in Sjögren's syndrome by SEREX
Uchida, K., Akita, Y., Matsuo, K., Fujiwara, S., Nakagawa, A., Kazaoka, Y., Hachiya, H., Naganawa, Y., Oh‐iwa, I., Ohura, K., et al. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02197.x · Cited by 72
Ohisa, S., Inohaya, K., Takano, Y., & Kudō, A. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.03.016 · Cited by 58
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Metadata
- Authors
- Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Baumgärtel, C., Schekman, R., & Rape, M.
- Affiliations
- University of California, Berkeley (US)
- Howard Hughes Medical Institute (US)
- Venue
- Nature
- Published
- 2012-02
- Volume
- 482
- Issue
- 7386
- Pages
- 495-500
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3292188
- OpenAlex
- W2050561023
- Cited by
- 330
- References
- 40
- Citations by year
- 2026: 12 · 2025: 18 · 2024: 14 · 2023: 17 · 2022: 26 · 2021: 21 · 2020: 25 · 2019: 15 · 2018: 25 · 2017: 25 · 2016: 27 · 2015: 26 · 2014: 25 · 2013: 42 · 2012: 11
- FWCI
- 15.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Foundation for the National Institutes of Health
- Howard Hughes Medical Institute
- National Institutes of Health (1dp2od003088-01)
- National Institute of General Medical Sciences (R01GM083064)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- COPII vesicles, monoubiquitylation, Sec31, ubiquitin ligase, chylomicron retention disease, ER-Golgi transport, protein secretion
- MeSH terms
- Animals, Cell Line, Collagen, HeLa Cells, Humans, Microfilament Proteins, Protein Transport, COP-Coated Vesicles, Ubiquitin, Vesicular Transport Proteins, Cullin Proteins, Cell Shape, Adaptor Proteins, Signal Transducing, Mice, Embryonic Stem Cells, Ubiquitination
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