V-ATPase is the dominant proton pump in plant cells. It contributes to cytosolic pH homeostasis and energizes transport processes across endomembranes of the secretory pathway.
Thorsten Seidel
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The role of individual domains and the significance of shedding of ATP6AP2/(pro)renin receptor in vacuolar H(+)-ATPase biogenesis. [PDF]
The ATPase 6 accessory protein 2 (ATP6AP2)/(pro)renin receptor (PRR) is essential for the biogenesis of active vacuolar H(+)-ATPase (V-ATPase). Genetic deletion of ATP6AP2/PRR causes V-ATPase dysfunction and compromises vesicular acidification.
Kenichiro Kinouchi +12 more
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Defining steps in RAVE-catalyzed V-ATPase assembly using purified RAVE and V-ATPase subcomplexes [PDF]
The vacuolar H+-ATPase (V-ATPase) is a highly conserved proton pump responsible for the acidification of intracellular organelles in virtually all eukaryotic cells. V-ATPases are regulated by the rapid and reversible disassembly of the peripheral V1 domain from the integral membrane Vo domain, accompanied by release of the V1 C subunit from both ...
Michael C. Jaskolka +4 more
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Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays. [PDF]
BACKGROUND:Vacuolar (H(+))-ATPase (V-ATPase; V(1)V(o)-ATPase) is a large multisubunit enzyme complex found in the endomembrane system of all eukaryotic cells where its proton pumping action serves to acidify subcellular organelles. In the plasma membrane
Lee S Parsons, Stephan Wilkens
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Molecular basis of mEAK7-mediated human V-ATPase regulation
Structural basis of V-ATPase regulation by endogenous proteins is unclear. Here, the authors find mEAK7 as an endogenous V-ATPase modulator and determine its structure with V-ATPase, suggesting the potential role of mEAK7 in V-ATPase regulation.
Rong Wang +3 more
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Enhanced expression of vacuolar H+-ATPase subunit E in the roots is associated with the adaptation of Broussonetia papyrifera to salt stress. [PDF]
Vacuolar H(+)-ATPase (V-H(+)-ATPase) may play a pivotal role in maintenance of ion homeostasis inside plant cells. In the present study, the expression of V-H(+)-ATPase genes was analyzed in the roots and leaves of a woody plant, Broussonetia papyrifera,
Min Zhang +3 more
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Vacuolar ATPase depletion contributes to dysregulation of endocytosis in bloodstream forms of Trypanosoma brucei [PDF]
BACKGROUND Vacuolar H-ATPase (V-ATPase) is a highly conserved protein complex which hydrolyzes ATP and pumps protons to acidify vacuolar vesicles.
Hide, G +4 more
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SNARE, V-ATPase et neurotransmission [PDF]
> La communication entre neurones repose principalement sur les synapses chimiques et par consequent sur la liberation de neurotransmetteurs. Au niveau des terminaisons nerveuses, des vesicules synaptiques remplies de neurotransmetteurs s’arriment a la membrane plasmique et subissent des etapes de maturation qui les rendent competentes pour la fusion ...
El Far, Oussama, Seagar, Michael
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The V-ATPase in insect epithelia [PDF]
![Figure][1] Mike O'Donnell discusses the impact of two classic papers, published by Helmut Wieczorek in Journal of Biological Chemistry in 1989 and 1991, which report the discovery of the the insect midgut V-ATPase.
Mike O'Donnell
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Vacuolar ATPase regulates surfactant secretion in rat alveolar type II cells by modulating lamellar body calcium. [PDF]
Lung surfactant reduces surface tension and maintains the stability of alveoli. How surfactant is released from alveolar epithelial type II cells is not fully understood. Vacuolar ATPase (V-ATPase) is the enzyme responsible for pumping H(+) into lamellar
Narendranath Reddy Chintagari +6 more
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