The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
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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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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