Proton translocation driven by ATP hydrolysis in V-ATPases.
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.
Kawasaki-Nishi
Shoko
S
Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, USA.
Nishi
Tsuyoshi
T
Forgac
Michael
M
D000227:Adenine Nucleotides / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D020134:Catalytic Domain; D006868:Hydrolysis; D017136:Ion Transport; D008954:Models, Biological; D021122:Protein Subunits; D006180:Proton-Translocating ATPases / Q000737:chemistry; D011522:Protons; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure
D000227:Adenine Nucleotides; D021122:Protein Subunits; D011522:Protons; D000255:Adenosine Triphosphate; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases