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<p>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 <i>Dictyostelium discoideum</i> 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.</p>

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The vault associates with membranes in situ

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年4月21日

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  • Katharina 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

摘要

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.