Kidney Vacuolar H+-ATPase: Physiology and Regulation

Patricia Valles, Michael S. Lapointe, Jan Wysocki, Daniel Batlle*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The vacuolar H+-ATPase is a multisubunit protein consisting of a peripheral catalytic domain (V1) that binds and hydrolyzes adenosine triphosphate (ATP) and provides energy to pump H+ through the transmembrane domain (V0) against a large gradient. This proton-translocating vacuolar H+-ATPase is present in both intracellular compartments and the plasma membrane of eukaryotic cells. Mutations in genes encoding kidney intercalated cell-specific V0 a4 and V1 B1 subunits of the vacuolar H+-ATPase cause the syndrome of distal tubular renal acidosis. This review focuses on the function, regulation, and the role of vacuolar H+-ATPases in renal physiology. The localization of vacuolar H+-ATPases in the kidney, and their role in intracellular pH (pHi) regulation, transepithelial proton transport, and acid-base homeostasis are discussed.

Original languageEnglish (US)
Pages (from-to)361-374
Number of pages14
JournalSeminars in nephrology
Volume26
Issue number5
DOIs
StatePublished - Sep 1 2006

Keywords

  • ATP6V0A4 subunit
  • ATP6V1B1 subunit
  • distal tubular renal acidosis (dRTA)
  • renal vacuolar H-ATPase

ASJC Scopus subject areas

  • Nephrology

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