The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP

  title={The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP},
  author={Jordi Querol-Audí and Arnau Casa{\~n}as and Isabel Us{\'o}n and Daniel Luque and Jos{\'e} R. Cast{\'o}n and Ignasi Fita and N{\'u}ria Verdaguer},
  journal={The EMBO Journal},
  pages={3450 - 3457}
Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel‐shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 Å resolution, together with the 2.1‐Å structure… 
Structural Dynamics of the Vault Ribonucleoprotein Particle
The high resolution, crystal structure of the of the seven N-terminal domains of MVP, forming the central vault barrel, revealed the interactions governing vault association and suggested a pH-dependent mechanism for a reversible dissociation induced by low pH.
Structural studies of large nucleoprotein particles, vaults
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Symmetry disruption commits vault particles to disassembly
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Solution Structures of Engineered Vault Particles
Vaults obtained by engineering at the N terminus of rat major vault protein an HIV-1 Gag protein segment are determined and their near-atomic resolution structures are determined in a solution/non-crystalline environment.
Bacterial Major Vault Protein homologs shed new light on origins of the enigmatic organelle
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The Vault Nanoparticle: A Gigantic Ribonucleoprotein Assembly Involved in Diverse Physiological and Pathological Phenomena and an Ideal Nanovector for Drug Delivery and Therapy
A better understanding of the physiological roles of this ribonucleoproteic complex may help develop new therapeutic strategies capable of coping with cancer progression and extend the scope of its exploitation as a nanocarrier for drug delivery.
New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach.
Re-refinement of the vault structure by incorporating the high-resolution information available for the R1-7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported.
Direct visualization of vaults within intact cells by electron cryo-tomography
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Structure of internalin InlK from the human pathogen Listeria monocytogenes.


Solution structure of a two-repeat fragment of major vault protein.
The Structure of Rat Liver Vault at 3.5 Angstrom Resolution
The x-ray structure of rat liver vault is determined at 3.5 angstrom resolution and it is shown that the cage structure consists of a dimer of half-vaults, with eachhalf-vault comprising 39 identical major vault protein (MVP) chains.
Structural domains of vault proteins: a role for the coiled coil domain in vault assembly.
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.
Cryoelectron microscopy imaging of recombinant and tissue derived vaults: localization of the MVP N termini and VPARP.
Structure of the vault, a ubiquitous celular component.
Structural stability of vault particles.
EM imaging showed the opening of intact vaults into flowerlike structures when transitioning from neutral to acidic pH, which has potential use in the development of recombinant vault into nanocapsules for drug delivery since one mechanism by which therapeutic agents entrapped in vaults could be released is through an opening of the intact vault structure.
Assembly of Vault-like Particles in Insect Cells Expressing Only the Major Vault Protein*
These particles are the first example of a single protein polymerizing into a non-spherically, non-cylindrically symmetrical structure and will enable us to design agents that disrupt vault formation and aid in elucidating vault functionin vivo.
Vaults and the major vault protein: Novel roles in signal pathway regulation and immunity
The current knowledge on MVP and vaults is reviewed with focus on regulatory functions in intracellular signal transduction and immune defence and the definition of precise vault functions is reviewed.
Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry
A structural model is proposed that predicts the stoichiometry of vault proteins and RNA, defines vault dimer-monomer interactions, and describes two possible modes for unfolding of vaults into flowers, likely to play a role in vault function.
Preliminary analysis of two and three dimensional crystals of vault ribonucleoprotein particles.