ArticleScience advances2022
Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The trial behind it
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- 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
- Review
- Sequence Determinants of Allosteric Back-to-front Control of the Arf Nucleotide Switch.Journal of molecular biology · 2025Article
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- Adaptor Protein Complexes in HIV-1 Pathogenesis: Mechanisms and Therapeutic Potential.Viruses · 2025Review
- Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025Review
- Virus infection and vesicle trafficking.Frontiers in immunology · 2025Review
- 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
- BEACH domain proteins function as cargo-sorting adaptors in secretory and endocytic pathways.The Journal of cell biology · 2024Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Article
- A structure-based mechanism for initiation of AP-3 coated vesicle formation.bioRxiv : the preprint server for biology · 2024Article
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1-positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection.
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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.