Major vault protein: Difference between revisions
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are the answer, what is the question? Trends Cell Biol. 6, 174 – 178.</ref> - around 90% within mammals <ref name=kesh> Kedersha, N. L., Miquel, M. C., Bittner, D., and Rome, L. H. (1990) Vaults. II. Ribonucleoprotein structures are highly conserved among higher and lower eukaryotes. J. Cell Biol. 110, 895 – 901. </ref> <ref name=mossink> Mossink, M. H., van Zon, A., Scheper, R. J.,Sonneveld, P., Wiemer, E. A., Schoester, M., Houtsmuller, A. B., Scheffer, G. L., Franzel-Luiten, E., Kickhoefer, V. A., Mossink, M., Poderycki, M. J., Chan, E. K., and Rome, L. H. (2003) Vaults: a ribonucleoprotein particle involved in drug resistance? Oncogene 22, 7458 – 7467.</ref> | are the answer, what is the question? Trends Cell Biol. 6, 174 – 178.</ref> - around 90% within mammals <ref name=kesh> Kedersha, N. L., Miquel, M. C., Bittner, D., and Rome, L. H. (1990) Vaults. II. Ribonucleoprotein structures are highly conserved among higher and lower eukaryotes. J. Cell Biol. 110, 895 – 901. </ref> <ref name=mossink> Mossink, M. H., van Zon, A., Scheper, R. J.,Sonneveld, P., Wiemer, E. A., Schoester, M., Houtsmuller, A. B., Scheffer, G. L., Franzel-Luiten, E., Kickhoefer, V. A., Mossink, M., Poderycki, M. J., Chan, E. K., and Rome, L. H. (2003) Vaults: a ribonucleoprotein particle involved in drug resistance? Oncogene 22, 7458 – 7467.</ref> | ||
There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+, but while it has been speculated that MVP contains at least two Ca2+-binding [[EF hand]]s in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene> <ref> Yu, Z., Fotouhi-Ardakani, N., Wu, L., Maoui, M., Wang, S., Banville, D., and Shen, S. H. (2002) PTEN associates with the vault particles in HeLa cells. J. Biol. Chem. 277, 40247 – 40252. </ref> , substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of <scene name='78/783129/Beta_loops/1'>acidic residues in the long β1/β2 and β2/β3 loops</scene> (Figure 1) of multiple MVP domains <ref> Kozlov, G., Vavelyuk, O., Minailiuc, O., Banville, D., Gehring, K., and Ekiel, I. (2006) Solution structure of a two-repeat fragment of major vault protein. J. Mol. Biol. 356, 444 – 452 </ref> , in a way similar to that found in[[ integrin]]s. | There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+, but while it has been speculated that MVP contains at least two Ca2+-binding [[EF hand]]s in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene> <ref> Yu, Z., Fotouhi-Ardakani, N., Wu, L., Maoui, M., Wang, S., Banville, D., and Shen, S. H. (2002) PTEN associates with the vault particles in HeLa cells. J. Biol. Chem. 277, 40247 – 40252. </ref> , substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of <scene name='78/783129/Beta_loops/1'>acidic residues in the long β1/β2 and β2/β3 loops</scene> (Figure 1) of multiple MVP domains <ref> Kozlov, G., Vavelyuk, O., Minailiuc, O., Banville, D., Gehring, K., and Ekiel, I. (2006) Solution structure of a two-repeat fragment of major vault protein. J. Mol. Biol. 356, 444 – 452 </ref> , in a way similar to that found in[[ integrin]]s. | ||
[[Image:Pdbnmr.jpg | thumb | '''Figure 1-''' The structure of the two domain fragment of MVP, depicted by NMR. Taken from the 1Y7X entry in the PBD. credit to: Kozlov, G., Vavelyuk, O., Minailiuc, O., Banville, D., Gehring, K., and Ekiel, I. (2006) Solution structure of a two-repeat fragment of major vault protein. J. Mol. Biol. 356, 444 – 452.]] | |||
==The MVP gene, transcription, translation and post translation modifications== | ==The MVP gene, transcription, translation and post translation modifications== | ||
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and vaults can be recruited to the nuclear envelope. Exp. Cell | and vaults can be recruited to the nuclear envelope. Exp. Cell | ||
Res. 312, 245 – 255. </ref>. | Res. 312, 245 – 255. </ref>. | ||
[[Image:Flower.jpg| thumb | Figure 2- The closed and open structures of MVP. Taken and modified from: Kickhoefer, V. A., Vasu, S. K., and Rome, L. H. (1996) Vaults | [[Image:Flower.jpg| thumb | '''Figure 2'''- The closed and open structures of MVP. Taken and modified from: Kickhoefer, V. A., Vasu, S. K., and Rome, L. H. (1996) Vaults | ||
are the answer, what is the question? Trends Cell Biol. 6, 174 – | are the answer, what is the question? Trends Cell Biol. 6, 174 – | ||
178.]] | 178.]] | ||
