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Title: Proton translocation driven by ATP hydrolysis in V-ATPases. Author: Kawasaki-Nishi S, Nishi T, Forgac M. Journal: FEBS Lett; 2003 Jun 12; 545(1):76-85. PubMed ID: 12788495. 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.[Abstract] [Full Text] [Related] [New Search]