Characterization of the Sea Urchin Major Vault Protein: A Possible Role for Vault Ribonucleoprotein Particles in Nucleocytoplasmic Transport

Hamill, Danielle R.; Suprenant, Kathy A.

doi:10.1006/dbio.1997.8676

Cited by 85 publications

(109 citation statements)

References 46 publications

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“…4A). Such distribution is consistent with the localization of MVP in the sea urchin embryo (Hamill & Suprenant 1997) and in other cell types (Chugani et al 1993). Cytoplasmic accumulation of the MVP in distinct patches and vesicle-like aggregates was observed in some of the abnormal IVF embryos, especially in those that underwent fragmentation during in vitro culture (e.g.…”

Section: Resultssupporting

confidence: 85%

“…To date, there is only one detailed study describing the expression and distribution of MVP in an animal, the sea urchin embryo (Hamill & Suprenant 1997), and one study identifying MVP as one of the proteins present in porcine egg extracts (Novak et al 2004). To our knowledge, no detailed studies of MVP exist for mammalian embryos, and it is not known whether MVP and the vault particles are present in mammalian embryo or whether they could play any role in mammalian development.…”

Section: Introductionmentioning

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

Reproduction

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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: Resultssupporting

confidence: 85%

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

Reproduction

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“…Vaults have been suggested to function in cytoplasmic transport, possibly via the microtubules (Hamill and Suprenant, 1997;Herrmann et al, 1999). The question arises as to what extent the microtubules are involved in the vaulttube formation.…”

Section: Integrity Of Microtubules Affects Vault-tube Formationmentioning

confidence: 99%

“…Nevertheless, a small part (~5%) of major vault protein (MVP) is consistently associated with the nucleus (Abbondanza et al, 1998;Chugani et al, 1993). Although the cellular function of vaults is still unknown, their subcellular localization and distinct morphology point to a role for vaults in intracellular, particularly nucleo-cytoplasmic, transport (Abbondanza et al, 1998;Chugani et al, 1993;Hamill and Suprenant, 1997;Herrmann et al, 1999;Herrmann et al, 1996;Kitazono et al, 2001;Kitazono et al, 1999;Li et al, 1999). Vaults are frequently upregulated in multidrug-resistant cell lines and tumors of different histogenetic origin.…”

Section: Introductionmentioning

confidence: 99%

The formation of vault-tubes: a dynamic interaction between vaults and vault PARP

Zon

Mossink

Schoester

et al. 2003

Journal of Cell Science

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tube-like structures in the cytoplasm. Raising the temperature could reverse this process. When the vaulttubes were formed, there were fewer or no VPARP-rods present in the cytoplasm, suggesting an incorporation of the VPARP into the vault-tubes. MVP molecules have to interact with each other via their coiled-coil domain in order to form vault-tubes. Furthermore, the stability of microtubules influenced the efficiency of vault-tube formation at 21°C. The dynamics and structure of the tubes were examined using confocal microscopy. Our data indicate a direct and dynamic relationship between vaults and VPARP, providing further clues to unravel the function of vaults.

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“…In Strongylocentrotus purpuratus eggs and two-cell embryos, a reconstituted microtubule-ribonucleoprotein (MT-RNP) complex consisting of ribosomes, microtubules, mRNA, 107-kDa major vault protein, 77-kDa EMAP, 80-and 66-kDa poly-A binding proteins, and an uncharacterized 100-kDa protein was isolated by temperature-and pHdependent polymerization cycling of MTs in cell extracts (Suprenant et al 1989;Hamill et al 1994;Hamill and Suprenant 1997). By electron microscopy, the MT-RNP complexes consisted of microtubule arrays studded with ribosomes that appeared to be connected via a salt-extractable, protease-sensitive stalk (Hamill et al 1994).…”

Section: Introductionmentioning

confidence: 99%

Seawi—a sea urchin piwi/argonaute family member is a component of MT-RNP complexes

Rodríguez¹,

Seipel²,

Hamill³

et al. 2005

RNA

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The piwi/argonaute family of proteins is involved in key developmental processes such as stem cell maintenance and axis specification through molecular mechanisms that may involve RNA silencing. Here we report on the cloning and characterization of the sea urchin piwi/argonaute family member seawi. Seawi is a major component of microtubule-ribonucleoprotein (MT-RNP) complexes isolated from two different species of sea urchin, Strongylocentrotus purpuratus and Paracentrotus lividus. Seawi co-isolates with purified ribosomes, cosediments with 80S ribosomes in sucrose density gradients, and binds microtubules. Seawi possesses the RNA binding motif common to piwi family members and binds P. lividus bep4 mRNA, a transcript that co-isolates with MT-RNP complexes and whose translation product has been shown to play a role in patterning the animal-vegetal axis. Indirect immunofluorescence studies localized seawi to the cortex of unfertilized eggs within granule-like particles, the mitotic spindle during cell division, and the small micromeres where its levels were enriched during the early cleavage stage. Lastly, we discuss how seawi, as a piwi/argonaute family member, may play a fundamentally important role in sea urchin animal-vegetal axis formation and stem cell maintenance.

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Characterization of the Sea Urchin Major Vault Protein: A Possible Role for Vault Ribonucleoprotein Particles in Nucleocytoplasmic Transport

Cited by 85 publications

References 46 publications

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

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

The formation of vault-tubes: a dynamic interaction between vaults and vault PARP

Seawi—a sea urchin piwi/argonaute family member is a component of MT-RNP complexes

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