Abstract:
V-ATPases are multisubunit ATP-dependent proton pumps consisting of two domains: a peripheral VI sector (subunits A-H), which binds and hydrolyses ATP, and a membrane-bound Vo sector (subunits a, c, c', c", d, and e), which forms the pore to proton transport. V 1 and Vo subunits are held together by one central stalk made of subunits D, F, and one (or two) peripheral stalks made of C, E, G, H and the N-end of subunit a. V-ATPases are essential in processes like urinary acidification, bone resorption, and pH homeostasis; therefore they are involved in diseases such as renal tubular acidosis, osteoporosis, and cancer invasiveness. As these processes involve the role of V-ATPases in pH regulation, this study uses the yeast Sacchromyces cerevisiae model system to explore V-ATPase proton pumps in vivo using phosphorus-3 1 NMR. The results addressing V-ATPase participation in adjusting intracellular pH are presented.