ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Structural mechanisms of cargo adaptors in membrane trafficking.Current opinion in cell biology · 2026Review
- Architecture of clathrin-independent AP3:ARF1-coated carriers.Science advances · 2026Article
- Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- PalKCH1 and PalKCH2 are required for tension wood formation and gelatinous layer deposition inFrontiers in plant science · 2026Article
- Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion.Sub-cellular biochemistry · 2026Review
- The Microbial Metabolite IDA Sensitizes Tumor Cells to ARF1 Inhibition by Inducing SVIL-dependent Senescence.International journal of biological sciences · 2026Article
- Review
- A structure-based mechanism for initiation of AP-3 coated vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A structure-based mechanism for initiation of AP-3 coated vesicle formation.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
- Erratum issued
- Update of
Authors and funding
15 authors.
Funding
Abstract
ADP-Ribosylation Factor (ARF) small GTPases have been found to act in vesicle fission through a direct ability to tubulate membrane. We have pursued cryoelectron microscopy (EM) to reveal at 3.9 Å resolution how ARF6 assembles into a protein lattice on tubulated membrane. Molecular dynamics simulation studies confirm and extend the cryo-EM findings. The ARF6 lattice exhibits features that are distinct from those formed by other membrane-bending proteins. We identify protein contacts critical for lattice assembly and how membrane insertion results in constricted tubules. The lattice structure also enables docking by GTPase-activating proteins (GAP) to achieve vesiculation. We have also modeled ARF1 onto the ARF6 lattice, and then pursued vesicle reconstitution by the Coat Protein I (COPI) complex to further confirm that the ARF lattice acts in vesicle fission. By elucidating how an ARF protein tubulates membrane at the structural level, we have advanced the molecular understanding of how this class of transport factors promote the fission stage of vesicle formation.
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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.