RNA location and modeling of a WD40 repeat domain within the vault.
@article{Kong2000RNALA, title={RNA location and modeling of a WD40 repeat domain within the vault.}, author={Lawrence B. Kong and Amara C. Siva and Valerie A. Kickhoefer and Leonard H. Rome and Phoebe L. Stewart}, journal={RNA}, year={2000}, volume={6 6}, pages={ 890-900 } }
The vault complex is a ubiquitous 13-MDa ribonucleoprotein assembly, composed of three proteins (TEP1, 240 kDa; VPARP, 193 kDa; and MVP, 100 kDa) that are highly conserved in eukaryotes and an untranslated RNA (vRNA). The vault has been shown to affect multidrug resistance in cancer cells, and one particular component, MVP, is thought to play a role in the transport of drug from the nucleus. To locate the position of the vRNA, vaults were treated with RNases, and cryo-electron microscopy (cryo…
72 Citations
Single Particle Reconstruction of the Vault from TEP1 Knockout Mice and Refinement of the Computationally Selected Vault Barrel
- BiologyMicroscopy and Microanalysis
- 2000
A published reconstruction of the intact rat vault at 31 Å resolution revealed that the vault complex is hollow and is structurally well suited to serve in macromolecular transport or sequestration.
Cryoelectron microscopy imaging of recombinant and tissue derived vaults: localization of the MVP N termini and VPARP.
- BiologyJournal of molecular biology
- 2004
Characterization of MVP and VPARP assembly into vault ribonucleoprotein complexes.
- BiologyBiochemical and biophysical research communications
- 2005
MVP and vaults: a role in the radiation response
- BiologyRadiation oncology
- 2011
New roles have been assigned to MVP and vaults including the association with the insulin-like growth factor-1, hypoxia-induciblefactor-1alpha, and the two major DNA double-strand break repair machineries: non-homologous endjoining and homologous recombination.
Structural domains of vault proteins: a role for the coiled coil domain in vault assembly.
- BiologyBiochemical and biophysical research communications
- 2002
This study identified and analyzed structural domains involved in vault assembly with emphasis on protein-protein interactions and demonstrated within MVP an intramolecular binding site and show that MVP molecules interact with each other via their coiled coil domain.
Structural studies of large nucleoprotein particles, vaults
- BiologyProceedings of the Japan Academy. Series B, Physical and biological sciences
- 2012
Vault is the largest nonicosahedral cytosolic nucleoprotein particle ever described. The widespread presence and evolutionary conservation of vaults suggest important biologic roles, although their…
Solution structure of a two-repeat fragment of major vault protein.
- BiologyJournal of molecular biology
- 2006
The formation of vault-tubes: a dynamic interaction between vaults and vault PARP
- BiologyJournal of Cell Science
- 2003
The subcellular localization and the dynamics of the vault complex in a non-small cell lung cancer cell line expressing MVP tagged with green fluorescent protein indicate a direct and dynamic relationship between vaults and VPARP, providing further clues to unravel the function of vaults.
Multiple Human Vault RNAs
- BiologyThe Journal of Biological Chemistry
- 2001
The findings suggest that vaults bind the RNA molecules with different affinities in different situations, and the ratio in which the vault RNAs are associated with vaults might be of functional importance.
Vaults: a ribonucleoprotein particle involved in drug resistance?
- BiologyOncogene
- 2003
The hollow barrel-shaped structure of the vault complex and its subcellular localization indicate a function in intracellular transport, and it was postulated that vaults contributed to drug resistance by transporting drugs away from their intrACEllular targets and/or the sequestration of drugs.
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