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PMID: 11836511 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

The vacuolar (H+)-ATPases--nature's most versatile proton pumps.

Nature reviews. Molecular cell biology ·Vol. 3 ·No. 2 ·2002-02-00 ·Pages 94-103

Nishi T, Forgac M

Abstract

The pH of intracellular compartments in eukaryotic cells is a carefully controlled parameter that affects many cellular processes, including intracellular membrane transport, prohormone processing and transport of neurotransmitters, as well as the entry of many viruses into cells. The transporters responsible for controlling this crucial parameter in many intracellular compartments are the vacuolar (H+)-ATPases (V-ATPases). Recent advances in our understanding of the structure and regulation of the V-ATPases, together with the mapping of human genetic defects to genes that encode V-ATPase subunits, have led to tremendous excitement in this field.

MeSH Terms
Cell Membrane/enzymology Humans Hydrogen-Ion Concentration Models, Biological Models, Molecular Molecular Structure Protein Subunits Proton-Translocating ATPases/chemistry,metabolism Vacuolar Proton-Translocating ATPases/chemistry,genetics,metabolism
Chemicals
Protein Subunits Vacuolar Proton-Translocating ATPases Proton-Translocating ATPases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nishi Tsuyoshi
Department of Physiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts 02111, USA.
Forgac Michael
Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0072
Published
2002-02-00
Pages
94-103
Language
English
Region
England
NLM ID
100962782
Subset
IM
Grants
NIGMS NIH HHS · R01 GM034478 · United States
NIGMS NIH HHS · R37 GM034478 · United States
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