ArticleBMC developmental biology2005
Sea urchin vault structure, composition, and differential localization during development.
Article in BMC developmental biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Vault Particles in Cancer Progression, Multidrug Resistance, and Drug Delivery: Current Insights and Future Applications.International journal of molecular sciences · 2025Review
- Major vault protein is part of an extracellular cement material in the Atlantic salmon louse (Lepeophtheirus salmonis).Scientific reports · 2024Article
- Vault RNAs (vtRNAs): Rediscovered non-coding RNAs with diverse physiological and pathological activities.Genes & diseases · 2024Review
- Major Vault Protein Inhibits Porcine Reproductive and Respiratory Syndrome Virus Infection in CRL2843Viruses · 2021Article
- Review
- 'High vault-age': non-coding RNA control of autophagy.Open biology · 2020Review
- In silico resurrection of the major vault protein suggests it is ancestral in modern eukaryotes.Genome biology and evolution · 2013Article
- Beyond BLASTing: tertiary and quaternary structure analysis helps identify major vault proteins.Genome biology and evolution · 2013Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
backgroundVaults are intriguing ribonucleoprotein assemblies with an unknown function that are conserved among higher eukaryotes. The Pacific coast sea urchin, Strongylocentrotus purpuratus, is an invertebrate model organism that is evolutionarily closer to humans than Drosophila and C. elegans, neither of which possesses vaults. Here we compare the structures of sea urchin and mammalian vaults and analyze the subcellular distribution of vaults during sea urchin embryogenesis.
resultsThe sequence of the sea urchin major vault protein (MVP) was assembled from expressed sequence tags and genome traces, and the predicted protein was found to have 64% identity and 81% similarity to rat MVP. Sea urchin MVP includes seven approximately 50 residue repeats in the N-terminal half of the protein and a predicted coiled coil domain in the C-terminus, as does rat MVP. A cryoelectron microscopy (cryoEM) reconstruction of isolated sea urchin vaults reveals the assembly to have a barrel-shaped external structure that is nearly identical to the rat vault structure. Analysis of the molecular composition of the sea urchin vault indicates that it contains components that may be homologs of the mammalian vault RNA component (vRNA) and protein components (VPARP and TEP1). The sea urchin vault appears to have additional protein components in the molecular weight range of 14-55 kDa that might correspond to molecular contents. Confocal experiments indicate a dramatic relocalization of MVP from the cytoplasm to the nucleus during sea urchin embryogenesis.
conclusionsThese results are suggestive of a role for the vault in delivering macromolecules to the nucleus during development.
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