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Cited by 55ATP Synthase and ATPases ResearchIon Transport and Channel RegulationCellular transport and secretion

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The Multifunctional Drosophila melanogaster V-ATPase Is Encoded by a Multigene Family

Dow, Julian A. T.·1999·Journal of Bioenergetics and Biomembranes
DOI 10.1023/a:1005400731289
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Abstract

In animals, V-ATPases are believed to play roles in the plasma membrane, as well as endomembrane. To understand these different functions, it is necessary to adopt a genetic approach in a physiologically tractable model organism. For this purpose, Drosophila melanogaster is ideal, because of the powerful genetics associated with the organism and because of the unusually informative epithelial phenotype provided by the Malpighian tubule. Recently, the first animal "knockouts" of a V-ATPase were described in Drosophila. The resulting phenotypes have general utility for our understanding of V-ATPase function and suggest a screen for novel subunits and associated proteins. Genome project resources have accelerated our knowledge of the V-ATPase gene family size and the new Drosophila genes vhaSFD, vha100-1, vha100-2, vha100-3, vha16-2, vha16-3, vha16-4, vhaPPA1, vhaPPA2, vhaM9.7.1, and vhaM9.7.2 are described. The Drosophila V-ATPase model is thus well-suited to both forward and reverse genetic analysis of this complex multifunctional enzyme.

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  1. Anraku, Y., Hirata, R., Wada, Y., and Ohya, Y. (1992). J. Exp. Biol. 172, 67–81. · DOI
  2. Ashburner, M., and Drysdale, R. (1994). Development 120, 2077–2079. · DOI
  3. Ballinger, D. G., and Benzer, S. (1989). Proc. Natl. Acad. Sci. USA 86, 9402–9406. · DOI
  4. Baron, R. (1995). Acta Orthopaed. Scand. 66, 66–70. · DOI
  5. Bellen, H. J., and Smith, R. F. (1995). Trends Genet 11, 456–457. · DOI
  6. Bowman, E. J., Tenney, K., and Bowman, B. J. (1988). J. Biol. Chem. 263, 13994–14001. · DOI
  7. Brand, A. H., and Perrimon, N. (1993). Development 118, 401–415. · DOI
  8. Brown, D., and Breton, S. (1996). J. Exp. Biol. 199, 2345–2358. · DOI
  9. Brown, D., Sabolic, I., and Gluck, S. (1992). J. Exp. Biol. 172, 231–243. · DOI
  10. Cooley, L., Kelley, R., and Spradling, A. (1988). Science 239, 1121–1128. · DOI
  11. Davies, S. A., Huesmann, G. R., Maddrell, S. H. P., O'Donnell, M. J., Skaer, N. J. V., Dow, J. A. T., and Tublitz, N. J. (1995). Am. J. Physiol. 269, R1321–R1326.
  12. Davies, S. A., Kelly, D. C., Goodwin, S. F., Wang, S.-Z., Kaiser, K., and Dow, J.A. T. (1996). J. Biol. Chem. 271, 30677–30684. · DOI
  13. Davies, S. A., Stewart, E. J., Heusmann, G. R., Skaer, N. J. V., Maddrell, S. H. P., Tublitz, N. J., and Dow, J. A. T. (1997). Am. J. Physiol. 273, R823–R827.
  14. Dow, J. A. T. (1984). Am. J. Physiol. 246, R633–R635.
  15. Dow, J. A. T. (1994). In Organellar Proton-ATPases (Nelson, N., ed.), R. G. Landes Company, Austin, TX, pp. 75–102.
  16. Dow, J. A. T., and Harvey, W. R. (1988). J. Exp. Biol. 140, 455–463. · DOI
  17. Dow, J. A. T., Maddrell, S. H. P., Davies, S.-A., Skaer, N. J. V., and Kaiser, K. (1994a). Am. J. Physiol. 266, R1716–R1719.
  18. Dow, J. A. T., Maddrell, S. H. P., Görtz, A., Skaer, N. V., Brogan, S., and Kaiser, K. (1994b). J. Exp. Biol. 197, 421–428. · DOI
  19. Dow, J. A. T., Davies, S. A., Guo, Y., Graham, S., Finbow, M. E., and Kaiser, K. (1997). J. Exp. Biol. 202, 237–245. · DOI
  20. Dow, J. A. T., Davies, S. A., and Sözen, M. A. (1998). Am. Zool. 38, 450–460. · DOI
  21. Ferea, T. L., and Bowman, B. J. (1996). Genetics 143, 147–154. · DOI
  22. Finbow, M. E., and Harrison, M. A. (1997). Biochem. J. 324, 697–712. · DOI
  23. Gausz, J., Bencze, G., Gyurkovics, H., Ashburner, M., Ish-Horowitz, D., and Holden, J. J. (1979). Genetics 93, 917–934. · DOI
  24. Gluck, S. (1992). J. Exp. Biol. 172, 29–37. · DOI
  25. Gluck, S. L., Underhill, D. M., Iyori, M., Holliday, L. S., Kostrominova, T. Y., and Lee, B. S. (1996). Annu. Rev. Physiol. 58, 427–445. · DOI
  26. Gogarten, J. P., Fichmann, J., Braun, Y., Morgan, L., Styles, P., Taiz, S. L., DeLapp, K., and Taiz, L. (1992). Plant Cell 4, 851–864.
  27. Guo, Y., Gillan, A., Töiök, T., Kiss, I., Dow, J. A. T., and Kaiser, K. (1996a). Genome Res. 6, 972–979. · DOI
  28. Guo, Y., Kaiser, K., Wieczorek, H., and Dow, J. A. T. (1996b). Gene 172, 239–243. · DOI
  29. Guo, Y., Wang, Z., Carter, A., Kaiser, K., and Dow, J. A. T. (1996c). Biochim. Biophys. Acta 1283, 4–9. · DOI
  30. Harvey, W. R., and Wieczorek, H. (1997). J. Exp. Biol. 200, 203–216. · DOI
  31. Harvey, W. R., Cioffi, M., and Wolfersberger, M. G. (1981). Am. Zool. 21, 775–791. · DOI
  32. Harvie, P. D., and Bryant, P. J. (1996). Conf. Drosophila Res. 37, 92.
  33. Hirata, R., Graham, L. A., Takatsuki, A., Stevens, T. H., and Anraku, Y. (1997). J. Biol. Chem. 272, 4795–4803. · DOI
  34. Kaiser, K., and Goodwin, S. F. (1990). Proc. Natl. Acad. Sci. USA 87, 1686–1690. · DOI
  35. Kane, P. M. (1992). J. Exp. Biol. 172, 93–103. · DOI
  36. Kato-Yamada, Y., Noji, H., Yasuda, R., Kinosita, K., Jr., and Yoshida, M. (1998). J Biol. Chem. 273, 19375–19377. · DOI
  37. Klein, U. (1992). J. Exp. Biol. 172, 345–354. · DOI
  38. Low, R., Rockel, B., Kirsch, M., Ratajczak, R., Hortensteiner, S., Martinoia, E., Luttge, U., and Rausch, T. (1996). Plant Physiol. 110, 259–265. · DOI
  39. Meagher, L., McLean, P., and Finbow, M. E. (1990). Nucleic Acids Res. 18, 6712. · DOI
  40. Mellman, I. (1992). J. Exp. Biol. 172, 39–45. · DOI
  41. Nelson, N., and Taiz, L. (1989). Trends Biochem. Sci. 14, 113–116. · DOI
  42. Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997). Nature 386, 299–302. · DOI
  43. Noumi, T., Beltran, C., Nelson, H., and Nelson, N. (1991). Proc. Natl. Acad. Sci. USA 88, 1938–1942. · DOI
  44. O'Donnell, M. J., Dow, J. A. T., Huesmann, G. R., Tublitz, N. J., and Maddrell, S. H. P. (1996). J. Exp. Biol. 199, 1163–1175. · DOI
  45. O'Donnell, M. J., Rheault, M. R., Davies, S. A., Rosay, P., Harvey, B. J., Maddrell, S. H. P., Kaiser, K., and Dow, J. A. T. (1998). Am. J. Physiol. 43, R1039–R1049.
  46. Petrov, D. A., and Hartl, D. L. (1997). Gene 205, 279–289. · DOI
  47. Rubin, G. M. (1988). Science 240, 1453–1459. · DOI
  48. Rubin, G. M. (1996). Genome Res 6, 71–79. · DOI
  49. Rubin, G. M. (1998). Trends Genet. 14, 340–343. · DOI
  50. Rubin, G. M., and Spradling, A. C. (1982). Science 218, 348–353. · DOI
  51. Ryerse, J. S. (1978). Nature 271, 745–746. · DOI
  52. Sözen, M. A., Armstrong, J. D., Yang, M. Y., Kaiser, K., and Dow, J. A. T. (1997). Proc. Natl. Acad. Sci. USA 94, 5207–5212. · DOI
  53. Spradling, A. C., Stern, D. M., Kiss, I., Roote, J., Laverty, T., and Rubin, G. M. (1995). Proc. Natl. Acad. Sci. USA 92, 10824–10830. · DOI
  54. Sumner, J. P., Dow, J. A. T., Earley, F., Klein, U., Jäger, D., and Wieczorek, H. (1995). J. Biol. Chem. 270, 5649–5653. · DOI
  55. Sze, H., Ward, J. M., Lai, S., and Perera, I. (1992). J. Exp. Biol. 172, 123–135. · DOI
  56. Wieczorek, H., and Harvey, W. R. (1995). Physiol. Zool. 68, 15–23. · DOI
  57. Wieczorek, H., Putzenlechner, M., Zeiske, W., and Klein, U. (1991). J. Biol. Chem. 266, 15340–15347. · DOI
  58. Yasuda, R., Noji, H., Kinosita, K., Jr., Motojima, F., and Yoshida, M. (1997). Bioenerg. Biomembr. 29, 207–209. · DOI
  59. Yasuda, R., Noji, H., Kinosita, K., Jr., and Yoshida, M. (1998). Cell 93, 1117–1124. · DOI

Cited by

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Metadata

Authors
Dow, J. A. T.
Affiliations
University of Glasgow (GB)
Corresponding author
Dow, Julian A. T.
ORCID
Dow, Julian A. T.
Venue
Journal of Bioenergetics and Biomembranes
Publisher
Springer Science and Business Media LLC
Published
1999-02
Volume
31
Issue
1
Pages
75-84
ISSN
  • 0145-479X (ISSN-L)
  • 1573-6881
DOI
10.1023/a:1005400731289
OpenAlex
W127681361
Cited by
55
References
0
Citations by year
2025: 1 · 2024: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2016: 3 · 2014: 1 · 2013: 4
FWCI
0.23
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Journal of Bioenergetics and Biomembranes (publishedVersion)
  • PubMed (publishedVersion)
Funders
Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
V-ATPase, Drosophila melanogaster, gene family, Malpighian tubules, knockout phenotypes, epithelial function
MeSH terms
Animals, DNA Mutational Analysis, Drosophila melanogaster, Multigene Family, Proton-Translocating ATPases, Vacuolar Proton-Translocating ATPases

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CoChat. (2026). Citation check: The Multifunctional Drosophila melanogaster V-ATPase Is Encoded by a Multigene Family. https://app.cochat.ai/papers/10.1023/a:1005400731289
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Dow, J. A. T. (1999). The Multifunctional Drosophila melanogaster V-ATPase Is Encoded by a Multigene Family. Journal of Bioenergetics and Biomembranes. https://doi.org/10.1023/a%3A1005400731289

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