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Evidence that vault ribonucleoprotein particles localize to the nuclear pore complex.
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.
PMID: 8270627 [PubMed - indexed for MEDLINE]
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Cited by 18 PubMed Central articles
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Role of drug transporters and drug accumulation in the temporal acquisition of drug resistance.
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[BMC Cancer. 2008]
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A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry.
Kato K, Tanaka H, Sumizawa T, Yoshimura M, Yamashita E, Iwasaki K, Tsukihara T.
Acta Crystallogr D Biol Crystallogr. 2008 May; 64(Pt 5):525-31. Epub 2008 Apr 19.
[Acta Crystallogr D Biol Crystallogr. 2008]
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Subtractive hybridization identifies novel differentially expressed ncRNA species in EBV-infected human B cells.
Mrázek J, Kreutmayer SB, Grässer FA, Polacek N, Hüttenhofer A.
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[Nucleic Acids Res. 2007]
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