A structural model of the vacuolar ATPase from transmission electron microscopy.
Vacuolar ATPases (V-ATPases) are large, membrane bound, multisubunit protein complexes which function as ATP hydrolysis driven proton pumps. V-ATPases and related enzymes are found in the endomembrane system of eukaryotic organsims, the plasma membrane of specialized cells in higher eukaryotes, and the plasma membrane of prokaryotes. The proton pumping action of the vacuolar ATPase is involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis, protein trafficking, active transport of metabolites, homeostasis and neurotransmitter release. This review summarizes recent progress in the structure determination of the vacuolar ATPase focusing on studies by transmission electron microscopy. A model of the subunit architecture of the vacuolar ATPase is presented which is based on the electron microscopic images and the available information from genetic, biochemical and biophysical experiments.
Wilkens
Stephan
S
Department of Biochemistry, University of California, Riverside, CA 92521, USA. stephan.wilkens@ucr.edu <stephan.wilkens@ucr.edu>
Zhang
Zhenyu
Z
Zheng
Yesha
Y
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000648:ultrastructure; D025262:Vacuolar Proton-Translocating ATPases / Q000648:ultrastructure*; D014617:Vacuoles / Q000201:enzymology / Q000648:ultrastructure
D025262:Vacuolar Proton-Translocating ATPases