ArticleCell reports2023
The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER.
Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- In situ cryo-ET defines the ultrastructure of ER exit sites in human cells.Nature cell biology · 2026Article
- Biomolecular Condensates in and Around the ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026Review
- Models of Intracellular Transport: Contradictions and Current Understanding.Sub-cellular biochemistry · 2026Review
- Mechanisms of COPII coat assembly and cargo recognition in the secretory pathway.Nature reviews. Molecular cell biology · 2025Review
- Review
- Organizing principles underlying COPII-mediated transport.Current opinion in cell biology · 2025Review
- Small GTPase ActIvitY ANalyzing (SAIYAN) system: A method to detect GTPase activation in living cells.The Journal of cell biology · 2024Article
- Tailored assemblies of COPII proteins in secretion.The Journal of cell biology · 2024Review
- Article
- TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.Molecular biology of the cell · 2024Article
- Protein condensates in the the secretory pathway: Unraveling biophysical interactions and function.Biophysical journal · 2024Review
- Article
- Functional overlap between the mammalianProceedings of the National Academy of Sciences of the United States of America · 2024Article
- HCMV US2 co-opts TRC8 to degrade the endoplasmic reticulum-resident protein LMAN2L.The Journal of general virology · 2024Article
- Functional overlap between the mammalianbioRxiv : the preprint server for biology · 2024Article
- Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport.Nature communications · 2023Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from discrete subdomains. Lipid bilayer remodeling necessary for this process is driven initially by membrane penetration mediated by the Sar1 GTPase and further stabilized by assembly of a multilayered complex of several COPII proteins. However, the relative contributions of these distinct factors to transport carrier formation and protein trafficking remain unclear. Here, we demonstrate that anterograde cargo transport from the ER continues in the absence of Sar1, although the efficiency of this process is dramatically reduced. Specifically, secretory cargoes are retained nearly five times longer at ER subdomains when Sar1 is depleted, but they ultimately remain capable of being translocated to the perinuclear region of cells. Taken together, our findings highlight alternative mechanisms by which COPII promotes transport carrier biogenesis.
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