ReviewJournal of bioenergetics and biomembranes1992
Vacuolar H(+)-translocating ATPases from plants: structure, function, and isoforms.
Review in Journal of bioenergetics and biomembranes, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 202 citations in OpenAlex.
- Relationships Among Arsenic-Related Traits, Including Rice Grain Arsenic Concentration and Straighthead Resistance, as Revealed by Genome-Wide Association.Frontiers in genetics · 2021Article
- Article
- New insights into regulation of proteome and polysaccharide in cell wall of Elsholtzia splendens in response to copper stress.PloS one · 2014Article
- Rapid structural changes and acidification of guard cell vacuoles during stomatal closure require phosphatidylinositol 3,5-bisphosphate.The Plant cell · 2013Article
- Plant-specific cation/H+ exchanger 17 and its homologs are endomembrane K+ transporters with roles in protein sorting.The Journal of biological chemistry · 2011Article
- pH dependence and inhibition by extracellular calcium of proton currents via plasmalemmal vacuolar-type H+-ATPase in murine osteoclasts.The Journal of physiology · 2006Article
- Article
- Differential expression of vacuolar H+-ATPase subunit c genes in tissues active in membrane trafficking and their roles in plant growth as revealed by RNAi.Plant physiology · 2004Article
- Historical perspective on microalgal and cyanobacterial acclimation to low- and extremely high-CO(2) conditions.Photosynthesis research · 2003Article
- Article
- Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Magnesium Sensitizes Slow Vacuolar Channels to Physiological Cytosolic Calcium and Inhibits Fast Vacuolar Channels in Fava Bean Guard Cell Vacuoles.Plant physiology · 1999Article
- Localization of a carboxylic residue possibly involved in the inhibition of vacuolar H+-pyrophosphatase by N, N'-dicyclohexylcarbodi-imide.The Biochemical journal · 1999Article
- Plant vacuolesThe Plant cell · 1999Article
- Energization of plant cell membranes by H+-pumping ATPases. Regulation and biosynthesisThe Plant cell · 1999Article
- cDNA and genomic cloning of sugar beet V-type H+-ATPase subunit A and c isoforms: evidence for coordinate expression during plant development and coordinate induction in response to high salinity.Plant molecular biology · 1999Article
- Structural aspects of the effectiveness of bisphosphonates as competitive inhibitors of the plant vacuolar proton-pumping pyrophosphatase.The Biochemical journal · 1999Article
- Initial steps in the assembly of the vacuole-type H+-ATPasePlant physiology · 1998Article
- Subunit interaction of vacuolar H+-pyrophosphatase as determined by high hydrostatic pressure.The Biochemical journal · 1998Article
- Amino acid carriers of Ricinus communis expressed during seedling development: molecular cloning and expression analysis of two putative amino acid transporters, RcAAP1 and RcAAP2.Plant molecular biology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vacuolar H(+)-translocating ATPase (V-type ATPase) plays a central role in the growth and development of plant cells. In a mature cell, the vacuole is the largest intracellular compartment, occupying about 90% of the cell volume. The proton electrochemical gradient (acid inside) formed by the vacuolar ATPase provides the primary driving force for the transport of numerous ions and metabolites against their electrochemical gradients. The uptake and release of solutes across the vacuolar membrane is fundamental to many cellular processes, such as osmoregulation, signal transduction, and metabolic regulation. Vacuolar ATPases may also reside on endomembranes, such as Golgi and coated vesicles, and thus may participate in intracellular membrane traffic, sorting, and secretion. Plant vacuolar ATPases are large complexes (400-650 kDa) composed of 7-10 different subunits. The peripheral sector of 5-6 subunits includes the nucleotide-binding catalytic and regulatory subunits of approximately 70 and approximately 60 kDa, respectively. Six copies of the 16-kDa proteolipid together with 1-3 other subunits make up the integral sector that forms the H+ conducting pathway. Isoforms of plant vacuolar ATPases are suggested by the variations in subunit composition observed among and within plant species, and by the presence of a small multigene family encoding the 16-kDa and 70-kDa subunits. Multiple genes may encode isoforms with specific properties required to serve the diverse functions of vacuoles and endomembrane compartments.
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