The Multifunctional Drosophila melanogaster V-ATPase Is Encoded by a Multigene Family
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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The screen identified Vha14, a subunit of the V1 head group of the vacuolar ATPase complex.
“Our screen also identified Vha14, a subunit of the V1 head group of the vacuolar ATPase (v-ATPase) complex that is required for lysosomal acidification (183).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [183]
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Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works
“Our screen also identified Vha14, a subunit of the V1 head group of the vacuolar ATPase (v-ATPase) complex that is required for lysosomal acidification (183).”
Background
- 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
- Published
- 1999-02
- Volume
- 31
- Issue
- 1
- Pages
- 75-84
- ISSN
- 0145-479X (ISSN-L)
- 1573-6881
- 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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