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Cited by 391

The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.

Regulation and Isoform Function of the V-ATPases

Open access
Toei, Masashi, Saum, Regina, Forgac, Michael·2010·Biochemistry
DOI 10.1021/bi100397s
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Abstract

The vacuolar (H(+))-ATPases are ATP-dependent proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane of eukaryotic cells. Intracellular V-ATPases play an important role in normal physiological processes such as receptor-mediated endocytosis, intracellular membrane trafficking, pro-hormone processing, protein degradation, and the coupled uptake of small molecules, such as neurotransmitters. They also function in the entry of various pathogenic agents, including many envelope viruses, like influenza virus, and toxins, like anthrax toxin. Plasma membrane V-ATPases function in renal pH homeostasis, bone resorption and sperm maturation, and various disease processes, including renal tubular acidosis, osteopetrosis, and tumor metastasis. V-ATPases are composed of a peripheral V(1) domain containing eight different subunits that is responsible for ATP hydrolysis and an integral V(0) domain containing six different subunits that translocates protons. In mammalian cells, most of the V-ATPase subunits exist in multiple isoforms which are often expressed in a tissue specific manner. Isoforms of one of the V(0) subunits (subunit a) have been shown to possess information that targets the V-ATPase to distinct cellular destinations. Mutations in isoforms of subunit a lead to the human diseases osteopetrosis and renal tubular acidosis. A number of mechanisms are employed to regulate V-ATPase activity in vivo, including reversible dissociation of the V(1) and V(0) domains, control of the tightness of coupling of proton transport and ATP hydrolysis, and selective targeting of V-ATPases to distinct cellular membranes. Isoforms of subunit a are involved in regulation both via the control of coupling and via selective targeting. This review will begin with a brief introduction to the function, structure, and mechanism of the V-ATPases followed by a discussion of the role of V-ATPase subunit isoforms and the mechanisms involved in regulation of V-ATPase activity.

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Metadata

Authors
Toei, M., Saum, R., & Forgac, M.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2010-05-19
Volume
49
Issue
23
Pages
4715-4723
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi100397s
OpenAlex
W2030677245
Cited by
391
References
91
FWCI
10.16
Type
journal article
Language
en
Open access
green

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