Vault Ribonucleoprotein Particles:  Sarcophagi, Gondolas, or Safety Deposit Boxes?

Suprenant, Kathy A.

doi:10.1021/bi026747e

Cited by 88 publications

(101 citation statements)

References 90 publications

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“…Subsequently, the MVP is regarded as an adverse prognostic factor for chemotherapy. Several functions of the vault particle have been proposed, including intracellular transport, assembly of ribonucleoprotein particles, and proteolytic degradation of ribonucleoproteins (reviewed by Suprenant 2002). Also suggestive of MVP's importance is the observation that the mutation of multiple MVP genes in Dictyostelium impedes cell growth under nutritional stress (Vasu et al 1993, Vasu & Rome 1995.…”

Section: Discussionmentioning

confidence: 99%

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Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Šutovský¹,

Manandhar²,

Laurinčík³

et al. 2005

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Major vault protein (MVP), also called lung resistance-related protein is a ribonucleoprotein comprising a major part (>70%) of the vault particle. The function of vault particle is not known, although it appears to be involved in multi-drug resistance and cellular signaling. Here we show that MVP is expressed in mammalian, porcine, and human ova and in the porcine preimplantation embryo. MVP was identified by matrix-assisted laser-desorption ionization-time-of-flight (MALDI-TOF) peptide sequencing and Western blotting as a protein accumulating in porcine zygotes cultured in the presence of specific proteasomal inhibitor MG132. MVP also accumulated in poor-quality human oocytes donated by infertile couples and porcine embryos that failed to develop normally after in vitro fertilization or somatic cell nuclear transfer. Normal porcine oocytes and embryos at various stages of preimplantation development showed mostly cytoplasmic labeling, with increased accumulation of vault particles around large cytoplasmic lipid inclusions and membrane vesicles. Occasionally, MVP was associated with the nuclear envelope and nucleolus precursor bodies. Nucleotide sequences with a high degree of homology to human MVP gene sequence were identified in porcine oocyte and endometrial cell cDNA libraries. We interpret these data as the evidence for the expression and ubiquitin-proteasome-dependent turnover of MVP in the mammalian ovum. Similar to carcinoma cells, MVP could fulfill a cell-protecting function during early embryonic development.

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Section: Discussionmentioning

confidence: 99%

“…The exact function of the vault particle or that of MVP is not known (reviewed by Suprenant 2002, van Zon et al 2003, though it appears to be involved in multi-drug resistance. MVP is increasingly expressed in certain carcinoma and leukemia cells that are refractory to drug treatment (chemotherapy).…”

Section: Introductionmentioning

confidence: 99%

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Šutovský¹,

Manandhar²,

Laurinčík³

et al. 2005

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“…MVP is the major structural component of vaults, a large and abundant RNA-protein complex found in most eukaryotic cells. Vaults form barrel-shaped hollow structures (13 MDa, ~55ϫ30 nm) consisting of ~96 molecules of MVP, two minor protein components (vault poly[ADP-ribose] polymerase and telomerase-associated protein-1) and about six copies of a small untranslated RNA (Suprenant, 2002;Mikyas et al, 2004;Anderson et al, 2007). MVP alone is sufficient to self-assemble into the characteristic vault structure (Stephen et al, 2001;Mikyas et al, 2004;Zheng et al, 2005).…”

Section: Mvp Is Associated With the Pore-inducing Membrane Fractionmentioning

confidence: 99%

“…MVP alone is sufficient to self-assemble into the characteristic vault structure (Stephen et al, 2001;Mikyas et al, 2004;Zheng et al, 2005). Remarkably, despite their ubiquitous expression, abundance and evolutionarily conservation, the function of vaults is still largely unknown (Suprenant, 2002;Steiner et al, 2006). Some authors found vaults to be enriched at the NPCs and implicated them in nucleocytoplasmic transport processes (Chugani et al, 1993;van Zon et al, 2006).…”

Section: Mvp Is Associated With the Pore-inducing Membrane Fractionmentioning

confidence: 99%

“…By contrast, the cell-free system used here is derived from purified subcellular fractions that might have lost compensatory mechanisms for NPC assembly. Participation of vaults in the fundamental process of NPC biogenesis, which in turn is tightly linked to cellular growth and proliferation processes, provides an explanation for the striking evolutionarily conservation of the MVP sequence and vault structure as well as the ubiquitous expression of vaults in normal cells and their upregulation in several tumor cells (Suprenant, 2002;Steiner et al, 2006).…”

Section: Recombinant Mvp and Purified Vault Complexes Both Promote Npmentioning

confidence: 99%

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Assembly of nuclear pore complexes mediated by major vault protein

Vollmar

Hacker

Zahedi

et al. 2009

Journal of Cell Science

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The experimental system Previously, we have noted that incubation of egg extract without addition of chromatin promoted the formation of flat membrane cisternae studded with pore complexes, termed annulate lamellae (AL) (Dabauvalle et al., 1991). In a subsequent study, we found that AL formation apparently depleted a specific type of membrane vesicles from the egg extract that were required for NPC assembly from the egg extract (Ewald et al., 1997). Once these pore-forming Supplementary material available online at

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