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TitleThe vault associates with membranes in situ.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateApr 21, 2026
AuthorsKatharina Geißler / Jan Philipp Kreysing / Yuning Wang / Desislava Glushkova / Agnieszka Obarska-Kosinska / Patrick C Hoffmann / Stefanie Böhm / Alexander Schmidt / Jakob Meier-Credo / Julian D Langer / Gerhard Hummer / Martin Beck /
PubMed AbstractThe eukaryotic vault particle is a giant ribonucleoprotein complex that assembles into an iconic barrel-like cage. Its cellular function has remained elusive despite extensive characterization. Using ...The eukaryotic vault particle is a giant ribonucleoprotein complex that assembles into an iconic barrel-like cage. Its cellular function has remained elusive despite extensive characterization. Using cryo-electron tomography of Dictyostelium discoideum cells, we define the distribution, structural states, and interaction landscape of vault particles in situ. Surprisingly, we detect a subpopulation of vault particles associated with the endoplasmic reticulum (ER) and nuclear envelope membranes. This association occurs at a defined barrel height of the vault particle. Membrane-associated particles appear to localize to patches of reduced membrane bilayer thickness and altered curvature. We further find that a fraction of vaults encloses 80S ribosomes in highly ordered orientations. These structural findings are further corroborated by proximity labeling experiments, which identify ER-resident proteins and numerous ribosomal components as vault particle interactors. The membrane-bound and ribosome-encapsulating vault populations that we uncover will direct future studies towards revealing vault function.
External linksNat Commun / PubMed:42014721 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution29.0 Å
Structure data

EMDB-56516: In situ Dictyostelium discoideum cytosolic vault
Method: EM (subtomogram averaging) / Resolution: 29.0 Å

Source
  • Dictyostelium discoideum AX2 (eukaryote)

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