2. Academic Validation
  3. Structure and Roles of V-type ATPases

Structure and Roles of V-type ATPases

  • Trends Biochem Sci. 2020 Apr;45(4):295-307. doi: 10.1016/j.tibs.2019.12.007.
Thamiya Vasanthakumar 1,  John L Rubinstein 2
Affiliations

Affiliations

  • 1 The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada; Department of Biochemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada. Electronic address: [email protected].
  • 2 The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada; Department of Biochemistry, The University of Toronto, Toronto, ON M5S 1A8, Canada; Department of Medical Biophysics, The University of Toronto, Toronto, ON M5G 1L7, Canada. Electronic address: [email protected].
PMID: 32001091 DOI: 10.1016/j.tibs.2019.12.007
Abstract

V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-driven proton pumps. V-ATPases are the primary source of organellar acidification in all eukaryotes, making them essential for many fundamental cellular processes. Enzymatic activity can be modulated by regulated and reversible disassembly of the complex, and several subunits of mammalian V-ATPase have multiple isoforms that are differentially localized. Although the biochemical properties of the different isoforms are currently unknown, mutations in specific subunit isoforms have been associated with various diseases, making V-ATPases potential drug targets. V-ATPase structure and activity have been best characterized in Saccharomyces cerevisiae, where recent structures have revealed details about the dynamics of the Enzyme, the proton translocation pathway, and conformational changes associated with regulated disassembly and autoinhibition.

Keywords

RAVE; V-ATPase; cryo-EM; isoform; yeast.

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