Structure and regulation of insect plasma membrane H(+)V-ATPase.
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. Second, midgut ion-tranport processes are strictly controlled by the regulation of the V-ATPase, which is the sole energizer of all ion transport in this epithelium. Recent advances in our understanding the structure of the V(1) and V(o) complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed.
Wieczorek
H
H
Department of Biology, University of Osnabrück, D-49069 Osnabrück, Germany. wieczorek@biologie.uni-osnabrueck.de
Grber
G
G
Harvey
W R
WR
Huss
M
M
Merzendorfer
H
H
Zeiske
W
W
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D006706:Homeostasis; D007814:Larva / Q000201:enzymology; D018402:Manduca / Q000201:enzymology*; D008854:Microscopy, Electron; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D025262:Vacuolar Proton-Translocating ATPases
D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases