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• W2160843443 endingPage "385" @default.
• W2160843443 startingPage "361" @default.
• W2160843443 abstract "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 expense of the proton-motive force (pmf), V-ATPases function exclusively as ATP-dependent proton pumps. The pmf generated by V-ATPases in organelles and membranes of eukaryotic cells is utilized as a driving force for numerous secondary transport processes. The mechanistic and structural relations between the two enzymes prompted us to suggest similar functional units in V-ATPase as was proposed to F-ATPase and to assign some of the V-ATPase subunit to one of four parts of a mechanochemical machine: a catalytic unit, a shaft, a hook, and a proton turbine. It was the yeast genetics that allowed the identification of special properties of individual subunits and the discovery of factors that are involved in the enzyme biogenesis and assembly. The V-ATPases play a major role as energizers of animal plasma membranes, especially apical plasma membranes of epithelial cells. This role was first recognized in plasma membranes of lepidopteran midgut and vertebrate kidney. The list of animals with plasma membranes that are energized by V-ATPases now includes members of most, if not all, animal phyla. This includes the classical Na + absorption by frog skin, male fertility through acidification of the sperm acrosome and the male reproductive tract, bone resorption by mammalian osteoclasts, and regulation of eye pressure. V-ATPase may function in Na + uptake by trout gills and energizes water secretion by contractile vacuoles in Dictyostelium. V-ATPase was first detected in organelles connected with the vacuolar system. It is the main if not the only primary energy source for numerous transport systems in these organelles. The driving force for the accumulation of neurotransmitters into synaptic vesicles is pmf generated by V-ATPase. The acidification of lysosomes, which are required for the proper function of most of their enzymes, is provided by V-ATPase. The enzyme is also vital for the proper function of endosomes and the Golgi apparatus. In contrast to yeast vacuoles that maintain an internal pH of ∼5.5, it is believed that the vacuoles of lemon fruit may have a pH as low as 2. Similarly, some brown and red alga maintain internal pH as low as 0.1 in their vacuoles. One of the outstanding questions in the field is how such a conserved enzyme as the V-ATPase can fulfill such diverse functions." @default.
• W2160843443 created "2016-06-24" @default.
• W2160843443 creator A5004977012 @default.
• W2160843443 creator A5085637404 @default.
• W2160843443 date "1999-04-01" @default.
• W2160843443 modified "2023-10-11" @default.
• W2160843443 title "Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases" @default.
• W2160843443 cites W124504601 @default.
• W2160843443 cites W147339078 @default.
• W2160843443 cites W1479799584 @default.
• W2160843443 cites W1482032523 @default.
• W2160843443 cites W1483874824 @default.
• W2160843443 cites W1484446060 @default.
• W2160843443 cites W1494174270 @default.
• W2160843443 cites W1494787191 @default.
• W2160843443 cites W1497077766 @default.
• W2160843443 cites W1497289365 @default.
• W2160843443 cites W1501217717 @default.
• W2160843443 cites W1503829526 @default.
• W2160843443 cites W1504256022 @default.
• W2160843443 cites W1508107852 @default.
• W2160843443 cites W1509504914 @default.
• W2160843443 cites W1517646929 @default.
• W2160843443 cites W1519338837 @default.
• W2160843443 cites W1519991061 @default.
• W2160843443 cites W1520576380 @default.
• W2160843443 cites W1521277810 @default.
• W2160843443 cites W1530844389 @default.
• W2160843443 cites W1532698739 @default.
• W2160843443 cites W1534168317 @default.
• W2160843443 cites W1535147323 @default.
• W2160843443 cites W1535401962 @default.
• W2160843443 cites W1537141010 @default.
• W2160843443 cites W1541312802 @default.
• W2160843443 cites W1542880421 @default.
• W2160843443 cites W1544439362 @default.
• W2160843443 cites W1551561822 @default.
• W2160843443 cites W1555092004 @default.
• W2160843443 cites W1556265505 @default.
• W2160843443 cites W1556766638 @default.
• W2160843443 cites W1557391975 @default.
• W2160843443 cites W1560944359 @default.
• W2160843443 cites W1562334062 @default.
• W2160843443 cites W156235783 @default.
• W2160843443 cites W1562371023 @default.
• W2160843443 cites W1566117661 @default.
• W2160843443 cites W1567706221 @default.
• W2160843443 cites W1567776138 @default.
• W2160843443 cites W1568817338 @default.
• W2160843443 cites W1573088096 @default.
• W2160843443 cites W1573476117 @default.
• W2160843443 cites W1574501720 @default.
• W2160843443 cites W1575239836 @default.
• W2160843443 cites W1577785183 @default.
• W2160843443 cites W1578236466 @default.
• W2160843443 cites W1578274745 @default.
• W2160843443 cites W1580000922 @default.
• W2160843443 cites W1582076669 @default.
• W2160843443 cites W1585892031 @default.
• W2160843443 cites W1591680865 @default.
• W2160843443 cites W1592537807 @default.
• W2160843443 cites W1596299677 @default.
• W2160843443 cites W1596316759 @default.
• W2160843443 cites W1596717338 @default.
• W2160843443 cites W1604460094 @default.
• W2160843443 cites W1604517711 @default.
• W2160843443 cites W1620220662 @default.
• W2160843443 cites W1625553880 @default.
• W2160843443 cites W1643128520 @default.
• W2160843443 cites W1647338923 @default.
• W2160843443 cites W1658143440 @default.
• W2160843443 cites W1666994550 @default.
• W2160843443 cites W1679092634 @default.
• W2160843443 cites W1833122216 @default.
• W2160843443 cites W1873059855 @default.
• W2160843443 cites W1901679321 @default.
• W2160843443 cites W1903233824 @default.
• W2160843443 cites W1937619740 @default.
• W2160843443 cites W1940626095 @default.
• W2160843443 cites W1940939086 @default.
• W2160843443 cites W1956952005 @default.
• W2160843443 cites W1961286497 @default.
• W2160843443 cites W1966301335 @default.
• W2160843443 cites W1966967267 @default.
• W2160843443 cites W1967213708 @default.
• W2160843443 cites W1967417100 @default.
• W2160843443 cites W1968576207 @default.
• W2160843443 cites W1971403296 @default.
• W2160843443 cites W1974781841 @default.
• W2160843443 cites W1977120851 @default.
• W2160843443 cites W1979031178 @default.
• W2160843443 cites W1980070945 @default.
• W2160843443 cites W1981270456 @default.
• W2160843443 cites W1982888120 @default.
• W2160843443 cites W1983837942 @default.
• W2160843443 cites W1984755904 @default.
• W2160843443 cites W1985335821 @default.
• W2160843443 cites W1986001368 @default.

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