Up-regulation of vaults may be necessary but not sufficient for multidrug resistance

Siva, Amara C.; Raval-Fernandes, Sujna; Stephen, Andrew; LaFemina, Michael J.; Scheper, Rik J.; Kickhoefer, Valerie A.; Rome, Leonard H.

doi:10.1002/1097-0215(200102)9999:9999<::aid-ijc1168>3.0.co;2-7

Cited by 81 publications

(69 citation statements)

References 48 publications

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“…Relatively high MVP expression levels associate with short VPARP-rods. When more MVP is present in a cell, more vault particles are formed (Siva et al, 2001;Stephen et al, 2001) and probably more VPARP is incorporated into these vaults. Consequently, less non-vault bound VPARP is present in the cell, leading to shorter VPARP-rods.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Protein samples were solubilized in SDS sample loading buffer, fractionated on 7.5% SDS-PAGE, and transferred to Hybond-C (Amersham Biosciences) by electroblotting. Western blots were performed using an anti-rat vault polyclonal antibody (N2), affinity purified anti-TEP1 polyclonal antibody, and affinity purified anti-VPARP polyclonal antibody as described previously (21). Reactive bands were detected using horseradish peroxidase-conjugated secondary antibody and visualized by ECL (Amersham Biosciences).…”

Section: Methodsmentioning

confidence: 99%

The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein

Kickhoefer

Poderycki

Chan

et al. 2002

Journal of Biological Chemistry

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Vaults are highly conserved ubiquitous ribonucleoprotein particles with an undefined function. Three protein species (p240/TEP1, p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault protein is sufficient to form the basic vault structure. Previously, we have shown that stable association of the vault RNA with the vault particle is dependent on its interaction with the p240/TEP1 protein. To identify other proteins that interact with the vault RNA, we used a UV-cross-linking assay. We find that a portion of the vault RNA is complexed with the La autoantigen in a separate smaller ribonucleoprotein particle. La interacts with the vault RNA (both in vivo and in vitro) presumably through binding to 3 -uridylates. Moreover, we also demonstrate that the La autoantigen is the 50-kDa protein that we have previously reported as a protein that co-purifies with vaults.

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“…The vault is also known to contain a noncoding RNA [vault RNA (vRNA); refs. [6][7][8][9][10][11]. Compared with the other components, the RNA represents <5% of the mass of the vault complex.…”

Section: Introductionmentioning

confidence: 99%

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Gopinath

Wadhwa

Kumar

2010

Molecular Cancer Research

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Several noncoding RNAs do vital cellular functions, including gene regulation and cell differentiation. Previously, we reported that vault RNA (vRNA) has the ability to recognize chemotherapeutic compounds, such as mitoxantrone, based on biophysical and biochemical analyses. In the present study, we show that human glioblastoma-, leukemia-, and osteocarcinoma-derived cell lines overexpress vRNA and exhibit higher resistance toward mitoxantrone. Interestingly, when vRNA expression was suppressed by RNA interference in these cells, the resistance progressively decreased. In agreement with these findings, overexpression of vRNA-1 caused resistance to mitoxantrone. These results suggest a role of vRNA in mitoxantrone resistance in malignant cells and justify further studies on the importance and application of noncoding RNAs in cancer chemotherapeutics. Mol Cancer Res; 8(11); 1536-46. ©2010 AACR.

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Up-regulation of vaults may be necessary but not sufficient for multidrug resistance

Cited by 81 publications

References 48 publications

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

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

The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

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