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Journal of Cell Science, Vol 106, Issue 1 23-29, Copyright © 1993 by Company of Biologists


JOURNAL ARTICLES

Evidence that vault ribonucleoprotein particles localize to the nuclear pore complex

DC Chugani, LH Rome and NL Kedersha
Department of Pharmacology, UCLA School of Medicine 90024.

Vaults are cytoplasmic ribonucleoprotein organelles that are highly conserved among diverse eukaryotic species. Their mass (12.9 MDa), diameter (26-35 nm) and shape (two halves, each with eightfold radial symmetry) have recently been determined and are similar to those ascribed to the central plug (or transporter) of the nuclear pore complex (NPC). The size and eightfold symmetry of the vault particle make it conducive to interacting physically in a complementary manner with NPCs. The present study demonstrates that vaults specifically associate with nuclei by both immunoblotting and immunofluorescence. Immunogold EM confirmed that vaults associate with the nuclear envelope in tissue sections and with NPCs of isolated nuclei.
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