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Renal Vacuolar H⁺-ATPase

Institute of Physiology, University of Zurich, Zurich, Switzerland; Departments of Genetics, Cellular and Molecular Physiology, and Surgery, School of Medicine, Yale University, New Haven, Connecticut; and Program in Membrane Biology, Renal Unit, Massachusetts General Hospital, Harvard University, Boston, Massachusetts

Vacuolar H⁺-ATPases are ubiquitous multisubunit complexes mediating the ATP-dependent transport of protons. In addition to their role in acidifying the lumen of various intracellular organelles, vacuolar H⁺-ATPases fulfill special tasks in the kidney. Vacuolar H⁺-ATPases are expressed in the plasma membrane in the kidney almost along the entire length of the nephron with apical and/or basolateral localization patterns. In the proximal tubule, a high number of vacuolar H⁺-ATPases are also found in endosomes, which are acidified by the pump. In addition, vacuolar H⁺-ATPases contribute to proximal tubular bicarbonate reabsorption. The importance in final urinary acidification along the collecting system is highlighted by monogenic defects in two subunits (ATP6V0A4, ATP6V1B1) of the vacuolar H⁺-ATPase in patients with distal renal tubular acidosis. The activity of vacuolar H⁺-ATPases is tightly regulated by a variety of factors such as the acid-base or electrolyte status. This regulation is at least in part mediated by various hormones and protein-protein interactions between regulatory proteins and multiple subunits of the pump.

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