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Journal articles on the topic 'V-ATPase'

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Published: 4 June 2021

Last updated: 9 March 2023

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1

Russell, V. E., U. Klein, M. Reuveni, D. D. Spaeth, M. G. Wolfersberger, and W. R. Harvey. "Antibodies to mammalian and plant V-ATPases cross react with the V-ATPase of insect cation-transporting plasma membranes." Journal of Experimental Biology 166, no. 1 (May 1, 1992): 131–43. http://dx.doi.org/10.1242/jeb.166.1.131.

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In immunobiochemical blots, polyclonal antibodies against subunits of plant and mammalian vacuolar-type ATPases (V-ATPases) cross-react strongly with corresponding subunits of larval Manduca sexta midgut plasma membrane V-ATPase. Thus, rabbit antiserum against Kalanchoe daigremontiana tonoplast V-ATPase holoenzyme cross-reacts with the 67, 56, 40, 28 and 20 kDa subunits of midgut V-ATPase separated by SDS-PAGE. Antisera against bovine chromaffin granule 72 and 39 kDa V-ATPase subunits cross-react with the corresponding 67 and 43 kDa subunits of midgut V-ATPase. Antisera against the 57 kDa subu

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2

Parra, Karlett J., Chun-Yuan Chan, and Jun Chen. "Saccharomyces cerevisiae Vacuolar H+-ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals." Eukaryotic Cell 13, no. 6 (April 4, 2014): 706–14. http://dx.doi.org/10.1128/ec.00050-14.

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ABSTRACTVacuolar H+-ATPases (V-ATPases) are highly conserved ATP-driven proton pumps responsible for acidification of intracellular compartments. V-ATPase proton transport energizes secondary transport systems and is essential for lysosomal/vacuolar and endosomal functions. These dynamic molecular motors are composed of multiple subunits regulated in part by reversible disassembly, which reversibly inactivates them. Reversible disassembly is intertwined with glycolysis, the RAS/cyclic AMP (cAMP)/protein kinase A (PKA) pathway, and phosphoinositides, but the mechanisms involved are elusive. The

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3

Collaco, Anne M., Peter Geibel, Beth S. Lee, John P. Geibel, and Nadia A. Ameen. "Functional vacuolar ATPase (V-ATPase) proton pumps traffic to the enterocyte brush border membrane and require CFTR." American Journal of Physiology-Cell Physiology 305, no. 9 (November 1, 2013): C981—C996. http://dx.doi.org/10.1152/ajpcell.00067.2013.

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Vacuolar ATPases (V-ATPases) are highly conserved proton pumps that regulate organelle pH. Epithelial luminal pH is also regulated by cAMP-dependent traffic of specific subunits of the V-ATPase complex from endosomes into the apical membrane. In the intestine, cAMP-dependent traffic of cystic fibrosis transmembrane conductance regulator (CFTR) channels and the sodium hydrogen exchanger (NHE3) in the brush border regulate luminal pH. V-ATPase was found to colocalize with CFTR in intestinal CFTR high expresser (CHE) cells recently. Moreover, apical traffic of V-ATPase and CFTR in rat Brunner's g

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4

Sautin, Yuri Y., Ming Lu, Andrew Gaugler, Li Zhang, and Stephen L. Gluck. "Phosphatidylinositol 3-Kinase-Mediated Effects of Glucose on Vacuolar H+-ATPase Assembly, Translocation, and Acidification of Intracellular Compartments in Renal Epithelial Cells." Molecular and Cellular Biology 25, no. 2 (January 15, 2005): 575–89. http://dx.doi.org/10.1128/mcb.25.2.575-589.2005.

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ABSTRACT Vacuolar H+-ATPases (V-ATPases) are a family of ATP-driven proton pumps. They maintain pH gradients between intracellular compartments and are required for proton secretion out of the cytoplasm. Mechanisms of extrinsic control of V-ATPase are poorly understood. Previous studies showed that glucose is an important regulator of V-ATPase assembly in Saccharomyces cerevisiae. Human V-ATPase directly interacts with aldolase, providing a coupling mechanism for glucose metabolism and V-ATPase function. Here we show that glucose is a crucial regulator of V-ATPase in renal epithelial cells and

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5

Gogarten, J. P., T. Starke, H. Kibak, J. Fishman, and L. Taiz. "Evolution and isoforms of V-ATPase subunits." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 137–47. http://dx.doi.org/10.1242/jeb.172.1.137.

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The structure of V- and F-ATPases/ATP synthases is remarkably conserved throughout evolution. Sequence analyses show that the V- and F-ATPases evolved from the same enzyme that was already present in the last common ancestor of all known extant life forms. The catalytic and non-catalytic subunits found in the dissociable head groups of both V-ATPases and F-ATPases are paralogous subunits, i.e. these two types of subunits evolved from a common ancestral gene. The gene duplication giving rise to these two genes (i.e. those encoding the catalytic and non-catalytic subunits) pre-dates the time of

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6

Kane, Patricia M. "The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase." Microbiology and Molecular Biology Reviews 70, no. 1 (March 2006): 177–91. http://dx.doi.org/10.1128/mmbr.70.1.177-191.2006.

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SUMMARY All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in organelle acidification. Not only is the structure of V-ATPases highly conserved among eukaryotes, but there are also many regulatory mechanisms that are similar between fungi and higher eukaryotes. These mechanisms allow cells both to regulate the pHs of different compartments and to respond to changing extracellular conditions. The Saccharomyces cerevisiae V-ATPase has emerged as an important model for V-ATPase structure and function in all eukaryotic cells. This review discusses current kno

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7

Nelson, Nathan, and William R. Harvey. "Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases." Physiological Reviews 79, no. 2 (April 1, 1999): 361–85. http://dx.doi.org/10.1152/physrev.1999.79.2.361.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It functions in almost every eukaryotic cell and energizes a wide variety of organelles and membranes. V-ATPases have similar structure and mechanism of action with F-ATPase and several of their subunits evolved from common ancestors. In eukaryotic cells, F-ATPases are confined to the semi-autonomous organelles, chloroplasts, and mitochondria, which contain their own genes that encode some of the F-ATPase subunits. In contrast to F-ATPases, whose primary function in eukaryotic cells is to form ATP at the expens

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8

Forgac, M. "Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 71–80. http://dx.doi.org/10.1242/jeb.203.1.71.

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The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps that carry out acidification of intracellular compartments in eukaryotic cells. This review is focused on our work on the V-ATPases of clathrin-coated vesicles and yeast vacuoles. The coated-vesicle V-ATPase undergoes trafficking to endosomes and synaptic vesicles, where it functions in receptor recycling and neurotransmitter uptake, respectively. The yeast V-ATPase functions to acidify the central vacuole and is necessary both for protein degradation and for coupled transport processes across the vacuolar memb

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9

Abe, Michiko, Mayu Saito, Ayana Tsukahara, Shuka Shiokawa, Kazuma Ueno, Hiroki Shimamura, Makoto Nagano, Junko Y. Toshima, and Jiro Toshima. "Functional complementation reveals that 9 of the 13 human V-ATPase subunits can functionally substitute for their yeast orthologs." Journal of Biological Chemistry 294, no. 20 (April 5, 2019): 8273–85. http://dx.doi.org/10.1074/jbc.ra118.006192.

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Vacuolar-type H+-ATPase (V-ATPase) is a highly conserved proton pump responsible for acidification of intracellular organelles and potential drug target. It is a multisubunit complex comprising a cytoplasmic V1 domain responsible for ATP hydrolysis and a membrane-embedded Vo domain that contributes to proton translocation across the membrane. Saccharomyces cerevisiae V-ATPase is composed of 14 subunits, deletion of any one of which results in well-defined growth defects. As the structure of V-ATPase and the function of each subunit have been well-characterized in yeast, this organism has been

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10

Imada, Katsumi, Tohru Minamino, Yumiko Uchida, Miki Kinoshita, and Keiichi Namba. "Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator." Proceedings of the National Academy of Sciences 113, no. 13 (March 16, 2016): 3633–38. http://dx.doi.org/10.1073/pnas.1524025113.

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FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar export apparatus, a member of the type III secretion system. The FliI6FliJ complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH homodimer binds to FliI to connect the ATPase complex to the flagellar base, but the details are unknown. Here we report the structure of the homodimer of a C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2shows an unusually asymmetric homodimeric structure that markedly resembles the peripheral stalk of the A/V-type ATPases. The FliHC2–FliI hexamer model

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11

Schep, Daniel G., Jianhua Zhao, and John L. Rubinstein. "Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance." Proceedings of the National Academy of Sciences 113, no. 12 (March 7, 2016): 3245–50. http://dx.doi.org/10.1073/pnas.1521990113.

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Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacterium Thermus thermophilus is similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined the T. thermophilus V/A-ATPase structure by cryo-EM at 6.4 Å resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequenc

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12

Rawson, Shaun, Michael A. Harrison, and Stephen P. Muench. "Rotating with the brakes on and other unresolved features of the vacuolar ATPase." Biochemical Society Transactions 44, no. 3 (June 9, 2016): 851–55. http://dx.doi.org/10.1042/bst20160043.

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The rotary ATPase family comprises the ATP synthase (F-ATPase), vacuolar ATPase (V-ATPase) and archaeal ATPase (A-ATPase). These either predominantly utilize a proton gradient for ATP synthesis or use ATP to produce a proton gradient, driving secondary transport and acidifying organelles. With advances in EM has come a significant increase in our understanding of the rotary ATPase family. Following the sub nm resolution reconstructions of both the F- and V-ATPases, the secondary structure organization of the elusive subunit a has now been resolved, revealing a novel helical arrangement. Despit

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13

Smardon, Anne M., Heba I. Diab, Maureen Tarsio, Theodore T. Diakov, Negin Dehdar Nasab, Robert W. West, and Patricia M. Kane. "The RAVE complex is an isoform-specific V-ATPase assembly factor in yeast." Molecular Biology of the Cell 25, no. 3 (February 2014): 356–67. http://dx.doi.org/10.1091/mbc.e13-05-0231.

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The regulator of ATPase of vacuoles and endosomes (RAVE) complex is implicated in vacuolar H+-translocating ATPase (V-ATPase) assembly and activity. In yeast, rav1∆ mutants exhibit a Vma− growth phenotype characteristic of loss of V-ATPase activity only at high temperature. Synthetic genetic analysis identified mutations that exhibit a full, temperature-independent Vma− growth defect when combined with the rav1∆ mutation. These include class E vps mutations, which compromise endosomal sorting. The synthetic Vma− growth defect could not be attributed to loss of vacuolar acidification in the dou

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14

Kane, P. M., and K. J. Parra. "Assembly and regulation of the yeast vacuolar H(+)-ATPase." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 81–87. http://dx.doi.org/10.1242/jeb.203.1.81.

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The yeast vacuolar H(+)-ATPase (V-ATPase) consists of a complex of peripheral subunits containing the ATP binding sites, termed the V(1) sector, attached to a complex of membrane subunits containing the proton pore, termed the V(o) sector. Interaction between the V(1) and V(o) sectors is essential for ATP-driven proton transport, and this interaction is manipulated in vivo as a means of regulating V-ATPase activity. When yeast (Saccharomyces cerevisiae) cells are deprived of glucose for as little as 5 min, up to 75% of the assembled V-ATPase complexes are disassembled into cytoplasmic V(1) sec

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15

Sennoune, Souad R., Karina Bakunts, Gloria M. Martínez, Jenny L. Chua-Tuan, Yamina Kebir, Mohamed N. Attaya, and Raul Martínez-Zaguilán. "Vacuolar H+-ATPase in human breast cancer cells with distinct metastatic potential: distribution and functional activity." American Journal of Physiology-Cell Physiology 286, no. 6 (June 2004): C1443—C1452. http://dx.doi.org/10.1152/ajpcell.00407.2003.

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Tumor cells thrive in a hypoxic microenvironment with an acidic extracellular pH. To survive in this harsh environment, tumor cells must exhibit a dynamic cytosolic pH regulatory system. We hypothesize that vacuolar H+-ATPases (V-ATPases) that normally reside in acidic organelles are also located at the cell surface, thus regulating cytosolic pH and exacerbating the migratory ability of metastatic cells. Immunocytochemical data revealed for the first time that V-ATPase is located at the plasma membrane of human breast cancer cells: prominent in the highly metastatic and inconspicuous in the lo

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16

Al-bataineh, Mohammad M., Fan Gong, Allison L. Marciszyn, Michael M. Myerburg, and Núria M. Pastor-Soler. "Regulation of proximal tubule vacuolar H+-ATPase by PKA and AMP-activated protein kinase." American Journal of Physiology-Renal Physiology 306, no. 9 (May 1, 2014): F981—F995. http://dx.doi.org/10.1152/ajprenal.00362.2013.

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The vacuolar H+-ATPase (V-ATPase) mediates ATP-driven H+ transport across membranes. This pump is present at the apical membrane of kidney proximal tubule cells and intercalated cells. Defects in the V-ATPase and in proximal tubule function can cause renal tubular acidosis. We examined the role of protein kinase A (PKA) and AMP-activated protein kinase (AMPK) in the regulation of the V-ATPase in the proximal tubule as these two kinases coregulate the V-ATPase in the collecting duct. As the proximal tubule V-ATPases have different subunit compositions from other nephron segments, we postulated

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17

Banerjee, Subhrajit, and Patricia M. Kane. "Direct interaction of the Golgi V-ATPase a-subunit isoform with PI(4)P drives localization of Golgi V-ATPases in yeast." Molecular Biology of the Cell 28, no. 19 (September 15, 2017): 2518–30. http://dx.doi.org/10.1091/mbc.e17-05-0316.

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Luminal pH and phosphoinositide content are fundamental features of organelle identity. Vacuolar H+-ATPases (V-ATPases) drive organelle acidification in all eukaryotes, and membrane-bound a-subunit isoforms of the V-ATPase are implicated in organelle-specific targeting and regulation. Earlier work demonstrated that the endolysosomal lipid PI(3,5)P2 activates V-ATPases containing the vacuolar a-subunit isoform in Saccharomyces cerevisiae. Here we demonstrate that PI(4)P, the predominant Golgi phosphatidylinositol (PI) species, directly interacts with the cytosolic amino terminal (NT) domain of

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18

Taiz, L. "THE PLANT VACUOLE." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 113–22. http://dx.doi.org/10.1242/jeb.172.1.113.

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Plant cells are unique in containing large acidic vacuoles which occupy most of the cell volume. The vacuolar H+-ATPase (V-ATPase) is the enzyme responsible for acidifying the central vacuole, although it is also present on Golgi and coated vesicles. Many secondary transport processes are driven by the proton-motive force generated by the V-ATPase, including reactions required for osmoregulation, homeostasis, storage, plant defense and many other functions. However, a second proton pump, the V-PPase, serves as a potential back-up system and may, in addition, pump potassium. The plant V-ATPase

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19

Obrdlik, Petr, Kerstin Diekert, Natalie Watzke, Christine Keipert, Ulrich Pehl, Catrin Brosch, Nicole Boehm, et al. "Electrophysiological characterization of ATPases in native synaptic vesicles and synaptic plasma membranes." Biochemical Journal 427, no. 1 (March 15, 2010): 151–59. http://dx.doi.org/10.1042/bj20091380.

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Vesicular V-ATPase (V-type H+-ATPase) and the plasma membrane-bound Na+/K+-ATPase are essential for the cycling of neurotransmitters at the synapse, but direct functional studies on their action in native surroundings are limited due to the poor accessibility via standard electrophysiological equipment. We performed SSM (solid supported membrane)-based electrophysiological analyses of synaptic vesicles and plasma membranes prepared from rat brains by sucrose-gradient fractionation. Acidification experiments revealed V-ATPase activity in fractions containing the vesicles but not in the plasma m

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20

Granger, D., M. Marsolais, J. Burry, and R. Laprade. "V-type H+-ATPase in the human eccrine sweat duct: immunolocalization and functional demonstration." American Journal of Physiology-Cell Physiology 282, no. 6 (June 1, 2002): C1454—C1460. http://dx.doi.org/10.1152/ajpcell.00319.2001.

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We investigated for the presence of a vacuolar-type H+-ATPase (V-ATPase) in the human eccrine sweat duct (SD). With the use of immunocytochemistry, an anti-V- ATPase antibody showed a strong staining at the apical membrane and a weaker one in the cytoplasm. Cold preservation followed by rewarming did not alter this staining pattern. With the use of the pH-sensitive dye 2′,7′-bis(2-carboxyethyl)-5(6)-carboxyfluorescein on isolated and perfused straight SD under HCO[Formula: see text]-free conditions and in the absence of Na+, proton extrusion was determined from the recovery rate of intracellul

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21

Grüber, G. "Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1Vo ATPases." Biochemical Society Transactions 33, no. 4 (August 1, 2005): 883–85. http://dx.doi.org/10.1042/bst0330883.

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V-ATPases (vacuolar ATPases) are responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are composed of a catalytic V1 sector, in which ATP hydrolysis takes place, and the Vo sector, which functions in proton conduction. The best established mechanism for regulating the V-ATPase activity in vivo involves reversible dissociation of the V1 and Vo domains, in which subunit C is intimately involved. In the last year, impressive progress has been made in elucidating the structure of the C subunit and i

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22

Allan, Adrian K., Juan Du, Shireen A. Davies, and Julian A. T. Dow. "Genome-wide survey of V-ATPase genes in Drosophila reveals a conserved renal phenotype for lethal alleles." Physiological Genomics 22, no. 2 (July 14, 2005): 128–38. http://dx.doi.org/10.1152/physiolgenomics.00233.2004.

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V-ATPases are ubiquitous, vital proton pumps that play a multiplicity of roles in higher organisms. In many epithelia, they are the major energizer of cotransport processes and have been implicated in functions as diverse as fluid secretion and longevity. The first animal knockout of a V-ATPase was identified in Drosophila, and its recessive lethality demonstrated the essential nature of V-ATPases. This article surveys the entire V-ATPase gene family in Drosophila, both experimentally and in silico. Adult expression patterns of most of the genes are shown experimentally for the first time, usi

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23

Holliday, L. Shannon. "Vacuolar H+-ATPase: An Essential Multitasking Enzyme in Physiology and Pathophysiology." New Journal of Science 2014 (January 23, 2014): 1–21. http://dx.doi.org/10.1155/2014/675430.

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Vacuolar H+-ATPases (V-ATPases) are large multisubunit proton pumps that are required for housekeeping acidification of membrane-bound compartments in eukaryotic cells. Mammalian V-ATPases are composed of 13 different subunits. Their housekeeping functions include acidifying endosomes, lysosomes, phagosomes, compartments for uncoupling receptors and ligands, autophagosomes, and elements of the Golgi apparatus. Specialized cells, including osteoclasts, intercalated cells in the kidney and pancreatic beta cells, contain both the housekeeping V-ATPases and an additional subset of V-ATPases, which

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Li, Sheena Claire, Theodore T. Diakov, Tao Xu, Maureen Tarsio, Wandi Zhu, Sergio Couoh-Cardel, Lois S. Weisman, and Patricia M. Kane. "The signaling lipid PI(3,5)P2 stabilizes V1–Vo sector interactions and activates the V-ATPase." Molecular Biology of the Cell 25, no. 8 (April 15, 2014): 1251–62. http://dx.doi.org/10.1091/mbc.e13-10-0563.

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Vacuolar proton-translocating ATPases (V-ATPases) are highly conserved, ATP-driven proton pumps regulated by reversible dissociation of its cytosolic, peripheral V1 domain from the integral membrane Vo domain. Multiple stresses induce changes in V1-Vo assembly, but the signaling mechanisms behind these changes are not understood. Here we show that certain stress-responsive changes in V-ATPase activity and assembly require the signaling lipid phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). V-ATPase activation through V1-Vo assembly in response to salt stress is strongly dependent on PI(3,5)P

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25

Wieczorek, H. "The insect V-ATPase, a plasma membrane proton pump energizing secondary active transport: molecular analysis of electrogenic potassium transport in the tobacco hornworm midgut." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 335–43. http://dx.doi.org/10.1242/jeb.172.1.335.

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Goblet cell apical membranes in the larval midgut of Manduca sexta are the site of active and electrogenic K+ secretion. They possess a vacuolar-type ATPase which, in its immunopurified form, consists of at least nine polypeptides. cDNAs for the A and B subunits screened by monoclonal antibodies to the A subunit of the Manduca V-ATPase or by hybridisation with a cDNA probe for a plant V-ATPase B subunit have been cloned and sequenced. There is a high degree of identity to the sequences of the respective subunits of other V-ATPases. The M. sexta plasma membrane V-ATPase is an electrogenic proto

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26

Pérez-Castiñeira, José R., Agustín Hernández, Rocío Drake, and Aurelio Serrano. "A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast." Biochemical Journal 437, no. 2 (June 28, 2011): 269–78. http://dx.doi.org/10.1042/bj20110447.

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V-ATPases (vacuolar H+-ATPases) are a specific class of multi-subunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. Another simpler proton pump that co-localizes with the V-ATPase occurs in plants and many protists: the single-subunit H+-PPase [H+-translocating PPase (inorganic pyrophosphatase)]. Little is known about the relative contribution of these two proteins to the acidification of intracellular compartments. In the present study, we show that the expression of a chimaeric derivative of the Arabidopsis thaliana H+-PPase AVP1, wh

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Sze, H., JM Ward, S. Lai, and I. Perera. "VACUOLAR-TYPE H+-TRANSLOCATING ATPases IN PLANT ENDOMEMBRANES: SUBUNIT ORGANIZATION AND MULTIGENE FAMILIES." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 123–35. http://dx.doi.org/10.1242/jeb.172.1.123.

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Acidification of endomembrane compartments by the vacuolar-type H+-translocating ATPase (V-ATPase) is vital to the growth and development of plants. The V-ATPase purified from oat roots is a large complex of 650x10(3 )Mr that contains 10 different subunits of 70, 60, 44, 42, 36, 32, 29, 16, 13 and 12x10(3 )Mr. This set of ten polypeptides is sufficient to couple ATP hydrolysis to proton pumping after reconstitution of the ATPase into liposomes. Unlike some animal V-ATPases, the purified and reconstituted V-ATPase from oat is directly stimulated by Cl-. The peripheral complex of the ATPase incl

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28

Sakai, Hiromu, Yoshie Moriura, Takuya Notomi, Junko Kawawaki, Keiko Ohnishi, and Miyuki Kuno. "Phospholipase C-dependent Ca2+-sensing pathways leading to endocytosis and inhibition of the plasma membrane vacuolar H+-ATPase in osteoclasts." American Journal of Physiology-Cell Physiology 299, no. 3 (September 2010): C570—C578. http://dx.doi.org/10.1152/ajpcell.00486.2009.

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In osteoclasts, elevation of extracellular Ca2+ is an endogenous signal that inhibits bone resorption. We recently found that an elevation of extracellular Ca2+ decreased proton extrusion through the plasma membrane vacuolar H+-ATPase (V-ATPase) rapidly. In this study we investigated mechanisms underlying this early Ca2+-sensing response, particularly in reference to the activity of the plasma membrane V-ATPase and to membrane retrieval. Whole cell clamp recordings allowed us to measure the V-ATPase currents and the cell capacitance ( Cm) simultaneously. Cm is a measure of cell surface. Extrac

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29

Bowman, E. J., and B. J. Bowman. "Cellular role of the V-ATPase in Neurospora crassa: analysis of mutants resistant to concanamycin or lacking the catalytic subunit A." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 97–106. http://dx.doi.org/10.1242/jeb.203.1.97.

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Vacuolar ATPases (V-ATPases) are large complex enzymes that are structural and mechanistic relatives of F(1)F(o)-ATPases. They hydrolyze ATP and pump protons across membranes to hyperpolarize membranes and, often, to acidify cellular compartments. The proton gradients generated are used to drive the movement of various compounds across membranes. V-ATPases are found in membranes of archaebacteria and some eubacteria, in various components of the endomembrane system of all eukaryotes and in the plasma membranes of many specialized eukaryotic cells. They have been implicated in a wide variety of

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30

Drory, Omri, and Nathan Nelson. "The Emerging Structure of Vacuolar ATPases." Physiology 21, no. 5 (October 2006): 317–25. http://dx.doi.org/10.1152/physiol.00017.2006.

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Bioenergetics and physiology of primary pumps have been revitalized by new insights into the mechanism of energizing biomembranes. Structural information is becoming available, and the three-dimensional structure of F-ATPase is being resolved. The growing understanding of the fundamental mechanism of energy coupling may revolutionize our view of biological processes. The F- and V-ATPases (vacuolar-type ATPase) exhibit a common mechanical design in which nucleotide-binding on the catalytic sector, through a cycle of conformation changes, drives the transmembrane passage of protons by turning a

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31

Wieczorek, H., G. Grber, W. R. Harvey, M. Huss, H. Merzendorfer, and W. Zeiske. "Structure and regulation of insect plasma membrane H(+)V-ATPase." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 127–35. http://dx.doi.org/10.1242/jeb.203.1.127.

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H(+) V-ATPases (V-ATPases) are found in two principal locations, in endomembranes and in plasma membranes. The plasma membrane V-ATPase from the midgut of larval Manduca sexta is the sole energizer of all transepithelial secondary transport processes. At least two properties make the lepidopteran midgut a model tissue for studies of general aspects of V-ATPases. First, it is a rich source for purification of the enzyme and therefore for structural studies: 20 larvae provide up to 0.5 mg of holoenzyme, and soluble, cytosolic V(1) complexes can be obtained in even greater amounts of up to 2 mg.

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32

Forgac, M. "Structure, function and regulation of the coated vesicle V-ATPase." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 155–69. http://dx.doi.org/10.1242/jeb.172.1.155.

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The coated vesicle V-ATPase plays an important role in both receptor-mediated endocytosis and intracellular membrane traffic by providing the acidic environment required for ligand-receptor dissociation and receptor recycling. The coated vesicle V-ATPase is a macromolecular complex of relative molecular mass 750,000 composed of nine subunits arranged in two structural domains. The peripheral V1 domain, which has a relative molecular mass of 500,000, has the subunit structure 73(3)58(3)40(1)34(1)33(1) and possesses all the nucleotide binding sites of the V-ATPase. The integral Vo domain of rela

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Nelson, N., N. Perzov, A. Cohen, K. Hagai, V. Padler, and H. Nelson. "The cellular biology of proton-motive force generation by V-ATPases." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 89–95. http://dx.doi.org/10.1242/jeb.203.1.89.

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The vacuolar H(+)-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It functions in almost every eukaryotic cell and energizes a wide variety of organelles and membranes. In contrast to F-ATPases, whose primary function in eukaryotic cells is to form ATP at the expense of the proton-motive force, V-ATPases function exclusively as ATP-dependent proton pumps. The proton-motive force generated by V-ATPases in organelles and across plasma membranes of eukaryotic cells is utilized as a driving force for numerous secondary transport processes. The enzyme is also vital for the prope

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Hinton, Ayana, Souad R. Sennoune, Sarah Bond, Min Fang, Moshe Reuveni, G. Gary Sahagian, Daniel Jay, Raul Martinez-Zaguilan, and Michael Forgac. "Function of a Subunit Isoforms of the V-ATPase in pH Homeostasis and in Vitro Invasion of MDA-MB231 Human Breast Cancer Cells." Journal of Biological Chemistry 284, no. 24 (April 14, 2009): 16400–16408. http://dx.doi.org/10.1074/jbc.m901201200.

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It has previously been shown that highly invasive MDA-MB231 human breast cancer cells express vacuolar proton-translocating ATPase (V-ATPases) at the cell surface, whereas the poorly invasive MCF7 cell line does not. Bafilomycin, a specific V-ATPase inhibitor, reduces the in vitro invasion of MB231 cells but not MCF7 cells. Targeting of V-ATPases to different cellular membranes is controlled by isoforms of subunit a. mRNA levels for a subunit isoforms were measured in MB231 and MCF7 cells using quantitative reverse transcription-PCR. The results show that although all four isoforms are detecta

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Gluck, S. L., R. D. Nelson, B. S. Lee, Z. Q. Wang, X. L. Guo, J. Y. Fu, and K. Zhang. "Biochemistry of the renal V-ATPase." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 219–29. http://dx.doi.org/10.1242/jeb.172.1.219.

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In most eukaryotic cells, vacuolar H(+)-ATPases (V-ATPases) are present primarily or exclusively in intracellular membrane compartments, functioning in the acidification of the endocytic and secretory vacuolar apparatus necessary for constitutive cell function. V-ATPases also participate in renal hydrogen ion secretion in both the proximal and distal nephron, residing at high concentrations on the plasma membrane, where they are regulated physiologically to maintain the acid-base balance of the organism. Recent experiments have begun to reveal how the kidney controls transcellular proton trans

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Klein, U. "THE INSECT V-ATPase, A PLASMA MEMBRANE PROTON PUMP ENERGIZING SECONDARY ACTIVE TRANSPORT: IMMUNOLOGICAL EVIDENCE FOR THE OCCURRENCE OF A V-ATPase IN INSECT ION-TRANSPORTING EPITHELIA." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 345–54. http://dx.doi.org/10.1242/jeb.172.1.345.

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Active electrogenic K+ transport in insects serves as the energy source for secretion or absorption in gastrointestinal epithelia or for the receptor current in sensory epithelia. In the larval midgut of the tobacco hornworm Manduca sexta, a vacuolar-type proton pump (V-ATPase) and a K+/nH+ antiport represent the functional elements of the potassium pump. Several immunological findings support the hypothesis that active K+ transport in other insect epithelia may also be energized by a V-ATPase. In immunoblots, crude homogenates of sensilla-rich antennae and Malpighian tubules of M. sexta cross

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Dane, Michaela, Kerstin Steinert, Kordula Esser, Susanne Bickel-Sandkötter, and Francisco Rodriguez-Valera. "Properties Of The Plasma Membrane Atpases Of The Halophilic Archaebacteria Haloferax Mediterranei And Haloferax Volcanii." Zeitschrift für Naturforschung C 47, no. 11-12 (December 1, 1992): 835–44. http://dx.doi.org/10.1515/znc-1992-11-1209.

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Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or Mn2+. The ATPases require high concentrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of Hf. mediterranei and Hf. volcanii, respectively, show different sensitivities to inhibitors of ATP hydrolysis. ATP hydrolysis of isolated Hf. mediterranei ATPase was inhibited by NaN3, which was reported to be specific for F-ATPases, by nitrate and N-ethylmaleimide (NEM),

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Casare, Fernando, Daiane Milan, and Ricardo Fernandez. "Stimulation of calcium-sensing receptor increases biochemical H+-ATPase activity in mouse cortex and outer medullary regions." Canadian Journal of Physiology and Pharmacology 92, no. 3 (March 2014): 181–88. http://dx.doi.org/10.1139/cjpp-2013-0256.

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The aim of this project was to investigate the interaction between the calcium-sensing receptor (CaSR) and proton extrusion by the V-ATPase and gastric-like isoform of the H+/K+-ATPase in the mouse nephron. Biochemical activity of H+- ATPases was analysed using a partially purified membrane fraction of mouse cortex and outer medullary region. The V-ATPase activity (sensitive to 10−7 mol·L−1 bafilomycin) from the cortical and outer medullary region was significantly stimulated by increasing the [Formula: see text] (outside Ca2+), in a dose-dependent pattern. Gastric H+/K+-ATPase activity (sensi

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Nolta, K. V., H. Padh, and T. L. Steck. "An immunocytochemical analysis of the vacuolar proton pump in Dictyostelium discoideum." Journal of Cell Science 105, no. 3 (July 1, 1993): 849–59. http://dx.doi.org/10.1242/jcs.105.3.849.

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Antisera were generated in rabbits against the vacuolar proton pump (V-H(+)-ATPase) purified from Dictyostelium discoideum. The antisera inhibited V-H(+)-ATPase but not F1-ATPase activity and immunoprecipitated and immunoblotted only the polypeptide subunits of the V-H(+)-ATPase from cell homogenates. Immunocytochemical analysis of intact cells and subcellular fractions showed that the predominant immunoreactive organelles were clusters of empty, irregular vacuoles of various sizes and shapes, which corresponded to the acidosomes. The cytoplasmic surfaces of lysosomes, phagosomes and the tubul

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Liberman, Rachel, Sarah Bond, Mara G. Shainheit, Miguel J. Stadecker, and Michael Forgac. "Regulated Assembly of Vacuolar ATPase Is Increased during Cluster Disruption-induced Maturation of Dendritic Cells through a Phosphatidylinositol 3-Kinase/mTOR-dependent Pathway." Journal of Biological Chemistry 289, no. 3 (November 22, 2013): 1355–63. http://dx.doi.org/10.1074/jbc.m113.524561.

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The vacuolar (H+)-ATPases (V-ATPases) are ATP-driven proton pumps composed of a peripheral V1 domain and a membrane-embedded V0 domain. Regulated assembly of V1 and V0 represents an important regulatory mechanism for controlling V-ATPase activity in vivo. Previous work has shown that V-ATPase assembly increases during maturation of bone marrow-derived dendritic cells induced by activation of Toll-like receptors. This increased assembly is essential for antigen processing, which is dependent upon an acidic lysosomal pH. Cluster disruption of dendritic cells induces a semi-mature phenotype assoc

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Păunescu, Teodor G., Leileata M. Russo, Nicolas Da Silva, Jana Kovacikova, Nilufar Mohebbi, Alfred N. Van Hoek, Mary McKee, Carsten A. Wagner, Sylvie Breton, and Dennis Brown. "Compensatory membrane expression of the V-ATPase B2 subunit isoform in renal medullary intercalated cells of B1-deficient mice." American Journal of Physiology-Renal Physiology 293, no. 6 (December 2007): F1915—F1926. http://dx.doi.org/10.1152/ajprenal.00160.2007.

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Mice deficient in the ATP6V1B1 (“B1”) subunit of the vacuolar proton-pumping ATPase (V-ATPase) maintain body acid-base homeostasis under normal conditions, but not when exposed to an acid load. Here, compensatory mechanisms involving the alternate ATP6V1B2 (“B2”) isoform were examined to explain the persistence of baseline pH regulation in these animals. By immunocytochemistry, the mean pixel intensity of apical B2 immunostaining in medullary A intercalated cells (A-ICs) was twofold greater in B1−/− mice than in B1+/+ animals, and B2 was colocalized with other V-ATPase subunits. No significant

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FINBOW, Malcolm E., and Michael A. HARRISON. "The vacuolar H+-ATPase: a universal proton pump of eukaryotes." Biochemical Journal 324, no. 3 (June 15, 1997): 697–712. http://dx.doi.org/10.1042/bj3240697.

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The vacuolar H+-ATPase (V-ATPase) is a universal component of eukaryotic organisms. It is present in the membranes of many organelles, where its proton-pumping action creates the low intra-vacuolar pH found, for example, in lysosomes. In addition, there are a number of differentiated cell types that have V-ATPases on their surface that contribute to the physiological functions of these cells. The V-ATPase is a multi-subunit enzyme composed of a membrane sector and a cytosolic catalytic sector. It is related to the familiar FoF1 ATP synthase (F-ATPase), having the same basic architectural const

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Sarafian, V., M. Potier, and R. J. Poole. "Radiation-inactivation analysis of vacuolar H+-ATPase and H+-pyrophosphatase from Beta vulgaris L. Functional sizes for substrate hydrolysis and for H+ transport." Biochemical Journal 283, no. 2 (April 15, 1992): 493–97. http://dx.doi.org/10.1042/bj2830493.

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The functional sizes of the vacuolar H(+)-ATPase (V-ATPase; EC 3.6.1.34) and H(+)-pyrophosphatase (PPase; EC 3.6.1.1) from vacuolar membranes of red beet (Beta vulgaris L.) were estimated by radiation inactivation, both for substrate hydrolysis and for H+ transport. For the V-ATPase, the radiation-inactivation size for H+ transport was 446 (403-497) kDa and that for ATP hydrolysis was 394 (359-435) kDa. The low values of both of these estimates suggest that not all subunits which may co-purify with V-ATPases are required for either hydrolysis or transport. For the PPase, the radiation-inactiva

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Dow, J. A., S. A. Davies, Y. Guo, S. Graham, M. E. Finbow, and K. Kaiser. "Molecular genetic analysis of V-ATPase function in Drosophila melanogaster." Journal of Experimental Biology 200, no. 2 (January 1, 1997): 237–45. http://dx.doi.org/10.1242/jeb.200.2.237.

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V-ATPases are phylogenetically widespread, highly conserved, multisubunit proton pumps. Originally characterised in endomembranes, they have been found to energise transport across plasma membranes in a range of animal cells and particularly in certain epithelia. While yeast is the model of choice for the rapid generation and identification of V-ATPase mutants, it does not allow their analysis in a plasma membrane context. For such purposes, Drosophila melanogaster is a uniquely suitable model. Accordingly, we have cloned and characterised genes encoding several V-ATPase subunits in D. melanog

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Zhou, Long, and Leonid A. Sazanov. "Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase." Science 365, no. 6455 (August 22, 2019): eaaw9144. http://dx.doi.org/10.1126/science.aaw9144.

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V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo–electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and

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Li, Ru, Shan Bai, Yuanyuan He, Qi Chen, Yanping Yao, Jinzi Wang, and Baoshan Chen. "Cpvma1, a Vacuolar H+-ATPase Catalytic Subunit of Cryphonectria parasitica, is Essential for Virulence and Hypovirus RNA Accumulation." Phytopathology® 109, no. 8 (August 2019): 1417–24. http://dx.doi.org/10.1094/phyto-08-18-0289-r.

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The vacuolar H+-ATPases (V-ATPases) are conserved ATP-dependent proton pumps that acidify intracellular compartments in eukaryotic cells. The role of Cpvma1, a V-ATPase catalytic subunit A of Cryphonectria parasitica, was investigated by generating cpvma1-overexpressing and cpvma1-silenced strains. The mutant strains were evaluated for phenotypic characteristics, V-ATPase activity, response to elevated pH and Ca2+ in the medium, virulence on chestnut, and accumulation of hypovirus RNA in the cells. Compared with the wild-type strain, cpvma1-overexpressing strains showed no significant differen

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Pérez-Sayáns, M., JM Suárez-Peñaranda, F. Barros-Angueira, PG Diz, JM Gándara-Rey, and A. García-García. "An update in the structure, function, and regulation of V-ATPases: the role of the C subunit." Brazilian Journal of Biology 72, no. 1 (February 2012): 189–98. http://dx.doi.org/10.1590/s1519-69842012000100023.

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Vacuolar ATPases (V-ATPases) are present in specialized proton secretory cells in which they pump protons across the membranes of various intracellular organelles and across the plasma membrane. The proton transport mechanism is electrogenic and establishes an acidic pH and a positive transmembrane potential in these intracellular and extracellular compartments. V-ATPases have been found to be practically identical in terms of the composition of their subunits in all eukaryotic cells. They have two distinct structures: a peripheral catalytic sector (V1) and a hydrophobic membrane sector (V0) r

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Vedovelli, Luca, John T. Rothermel, Karin E. Finberg, Carsten A. Wagner, Anie Azroyan, Eric Hill, Sylvie Breton, Dennis Brown, and Teodor G. Păunescu. "Altered V-ATPase expression in renal intercalated cells isolated from B1 subunit-deficient mice by fluorescence-activated cell sorting." American Journal of Physiology-Renal Physiology 304, no. 5 (March 1, 2013): F522—F532. http://dx.doi.org/10.1152/ajprenal.00394.2012.

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Unlike human patients with mutations in the 56-kDa B1 subunit isoform of the vacuolar proton-pumping ATPase (V-ATPase), B1-deficient mice (Atp6v1b1−/−) do not develop metabolic acidosis under baseline conditions. This is due to the insertion of V-ATPases containing the alternative B2 subunit isoform into the apical membrane of renal medullary collecting duct intercalated cells (ICs). We previously reported that quantitative Western blots (WBs) from whole kidneys showed similar B2 protein levels in Atp6v1b1−/− and wild-type mice (Păunescu TG, Russo LM, Da Silva N, Kovacikova J, Mohebbi N, Van H

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Mccarty, RE. "A PLANT BIOCHEMIST'S VIEW OF H+-ATPases AND ATP SYNTHASES." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 431–41. http://dx.doi.org/10.1242/jeb.172.1.431.

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My twenty-five year fascination with membrane ATPases grew out of my experiences in the laboratories of André Jagendorf and Efraim Racker. André introduced me to photosynthetic phosphorylation and Ef, to whose memory this article is dedicated, convinced me that ATPases had much to do with ATP synthesis. Astounding progress has been made in the H+-ATPase field in just two decades. By the early 1970s, it was generally recognized that oxidative and photosynthetic ATP synthesis were catalyzed by membrane enzymes that could act as H+-ATPases and that the common intermediate between electron transpo

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Xie, Xiao-Song, David Padron, Xibin Liao, Jin Wang, Michael G. Roth, and Jef K. De Brabander. "Salicylihalamide A Inhibits the V0Sector of the V-ATPase through a Mechanism Distinct from Bafilomycin A1." Journal of Biological Chemistry 279, no. 19 (March 3, 2004): 19755–63. http://dx.doi.org/10.1074/jbc.m313796200.

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The newly identified specific V-ATPase inhibitor, salicylihalamide A, is distinct from any previously identified V-ATPase inhibitors in that it inhibits only mammalian V-ATPases, but not those from yeast or other fungi (Boyd, M. R., Farina, C., Belfiore, P., Gagliardi, S., Kim, J. W., Hayakawa, Y., Beutler, J. A., McKee, T. C., Bowman, B. J., and Bowman, E. J. (2001)J. Pharmacol. Exp. Ther.297, 114–120). In addition, salicylihalamide A does not compete with concanamycin or bafilomycin for binding to V-ATPase, indicating that it has a different binding site from those classic V-ATPase inhibitor

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