Cited by 330Cellular transport and secretionUbiquitin and proteasome pathwaysEndoplasmic Reticulum Stress and Disease

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Ubiquitin-dependent regulation of COPII coat size and function

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Jin, Lingyan, Pahuja, Kanika Bajaj, Wickliffe, Katherine E., Gorur, Amita, Baumgärtel, Christine, Schekman, Randy, Rape, Michael·2012·Nature

DOI 10.1038/nature10822PMC PMC3292188

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Abstract

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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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)
ORCID: Pahuja, Kanika Bajaj
Schekman, Randy
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2012-02
Volume: 482
Issue: 7386
Pages: 495-500
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature10822
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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Ubiquitin-dependent regulation of COPII coat size and function

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