Proton translocation driven by ATP hydrolysis in V-ATPases |
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Authors: | Kawasaki-Nishi Shoko Nishi Tsuyoshi Forgac Michael |
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Affiliation: | Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, USA. |
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Abstract: | The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubunit complexes composed of a peripheral domain (V(1)) responsible for ATP hydrolysis and an integral domain (V(0)) responsible for proton translocation. Based upon their structural similarity to the F(1)F(0) ATP synthases, the V-ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V(1) drives rotation of a ring of proteolipid subunits in V(0). This review is focused on the current structural knowledge of the V-ATPases as it relates to the mechanism of ATP-driven proton translocation. |
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Keywords: | V-ATPase Vacuolar acidification Proton transport ATP hydrolysis Mechanism |
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