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The vault associates with membranes in situ

ABSTRACT: 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. Those 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.

INSTRUMENT(S):

ORGANISM(S): Dictyostelium Discoideum (slime Mold)

SUBMITTER: Julian Langer

LAB HEAD: Julian Langer

PROVIDER: PXD071329 | Pride | 2026-04-21

REPOSITORIES: Pride

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			Action	DRS
	250319_pepsep15C_25min_pydiaid_bulk_19_C_01_Slot1-03_1_5079.d.zip	Other
	250319_pepsep15C_25min_pydiaid_bulk_19_C_02_Slot1-15_1_5087.d.zip	Other
	250319_pepsep15C_25min_pydiaid_bulk_19_C_03_Slot1-27_1_5095.d.zip	Other
	250319_pepsep15C_25min_pydiaid_bulk_19_C_04_Slot1-39_1_5105.d.zip	Other
	250319_pepsep15C_25min_pydiaid_bulk_19_C_05_Slot1-51_1_5118.d.zip	Other

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