ArticleJournal of bioenergetics and biomembranes2008
The d subunit plays a central role in human vacuolar H(+)-ATPases.
Article in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Association and functional study ofWorld journal of psychiatry · 2025Article
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- Article
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- Perfusion of isolated rat kidney with Mesenchymal Stromal Cells/Extracellular Vesicles prevents ischaemic injury.Journal of cellular and molecular medicine · 2017Article
- Regulation and isoform function of the V-ATPases.Biochemistry · 2010Review
- The vacuolar proton pump, V-ATPase, is required for notch signaling and endosomal trafficking in Drosophila.Developmental cell · 2009Article
- Cloning and sequencing of V-ATPase subunit d from mung bean and its function in passive proton transport.Journal of bioenergetics and biomembranes · 2008Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The multi-subunit vacuolar-type H(+)-ATPase consists of a V(1) domain (A-H subunits) catalyzing ATP hydrolysis and a V(0) domain (a, c, c', c", d, e) responsible for H(+) translocation. The mammalian V(0) d subunit is one of the least-well characterized, and its function and position within the pump are still unclear. It has two different forms encoded by separate genes, d1 being ubiquitous while d2 is predominantly expressed at the cell surface in kidney and osteoclast. To determine whether it forms part of the pump's central stalk as suggested by bacterial A-ATPase studies, or is peripheral as hypothesized from a yeast model, we investigated both human d subunit isoforms. In silico structural modelling demonstrated that human d1 and d2 are structural orthologues of bacterial subunit C, despite poor sequence identity. Expression studies of d1 and d2 showed that each can pull down the central stalk's D and F subunits from human kidney membrane, and in vitro studies using D and F further showed that the interactions between these proteins and the d subunit is direct. These data indicate that the d subunit in man is centrally located within the pump and is thus important in its rotary mechanism.
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