ArticleStructure (London, England : 1993)2025
Cryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps.
Article in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Article
- TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026Article
- Structural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations.Nature communications · 2026Article
- The vault associates with membranes in situ.Nature communications · 2026Article
- The vault particle is enclosed by aScience advances · 2026Article
- Structures of human organellar SPFH protein complexes.Nature communications · 2025Article
- Cryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps.Structure (London, England : 1993) · 2025Article
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Authors and funding
2 authors.
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Abstract
The vault protein is expressed in most eukaryotic cells, where it is assembled on polyribosomes into large hollow barrel-shaped complexes. Despite its widespread and abundant presence in cells, the biological function of the vault remains unclear. In this study, we describe the cryo-EM structure of vault particles that were imaged as a contamination of a preparation to extract tau filaments from brain tissue of an individual with progressive supranuclear palsy (PSP). We identify a mechanism of symmetry mismatch at the caps of the vault, from 39-fold to 13-fold symmetry, where two out of three monomers are sequentially excluded from the cap, resulting in a narrow, greasy pore at the tip of the vault. Our structure offers valuable insights for engineering carboxy-terminal modifications of the major vault protein (MVP) for potential therapeutic applications.
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