ArticleStructure (London, England : 1993)2021
Structural basis for the initiation of COPII vesicle biogenesis.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Avl9 defines a family of DENN domain GTPase-activating proteins.The Journal of cell biology · 2026Article
- Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations.Nucleic acids research · 2026Article
- Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026Review
- Classification and biogenesis of vesicles, and their roles in the transport of viral components.Archives of microbiology · 2026Review
- Avl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functions.bioRxiv : the preprint server for biology · 2026Article
- Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- Defective anterograde protein-trafficking contributes to endoplasmic reticulum-stress in a CLN1 disease model.Neurobiology of disease · 2025Article
- Potential ER tubular lumen sensing by intrinsically disordered regions.Journal of cell science · 2025Article
- C9orf72 controls hepatic lipid metabolism by regulating SREBP1 transport.Cell death and differentiation · 2024Article
- COPII cage assembly factor Sec13 integrates information flow regulating endomembrane function in response to human variation.Scientific reports · 2024Article
- Activity-based directed evolution of a membrane editor in mammalian cells.Nature chemistry · 2023Article
- Sec16 and Sed4 interdependently function as interaction and localization partners at ER exit sites.Journal of cell science · 2023Article
- The alarmone ppGpp selectively inhibits the isoform A of the human small GTPase Sar1.Proteins · 2023Article
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- Comment on Dimou et al. Profile of Membrane Cargo Trafficking Proteins and Transporters Expressed under N Source Derepressing Conditions inJournal of fungi (Basel, Switzerland) · 2021Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The first stage of the eukaryotic secretory pathway is the packaging of cargo proteins into coat protein complex II (COPII) vesicles exiting the ER. The cytoplasmic COPII vesicle coat machinery is recruited to the ER membrane by the activated, GTP-bound, form of the conserved Sar1 GTPase. Activation of Sar1 on the surface of the ER by Sec12, a membrane-anchored GEF (guanine nucleotide exchange factor), is therefore the initiating step of the secretory pathway. Here we report the structure of the complex between Sar1 and the cytoplasmic GEF domain of Sec12, both from Saccharomyces cerevisiae. This structure, representing a key nucleotide-free activation intermediate, reveals how the potassium ion-binding K loop disrupts the nucleotide-binding site of Sar1. We propose an unexpected orientation of the GEF domain relative to the membrane surface and postulate a mechanism for how Sec12 facilitates membrane insertion of the amphipathic helix exposed by Sar1 upon GTP binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.