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Cited by 337ATP Synthase and ATPases ResearchIon Transport and Channel RegulationHeat shock proteins research

Recent Insights into the Structure, Regulation, and Function of the V-ATPases

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Cotter, Kristina, Stransky, Laura, McGuire, Christina, Forgac, Michael·2015·Trends in Biochemical Sciences
DOI 10.1016/j.tibs.2015.08.005PMC PMC4589219
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Abstract

The vacuolar (H(+))-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular compartments and are also present at the plasma membrane. They function in such processes as membrane traffic, protein degradation, virus and toxin entry, bone resorption, pH homeostasis, and tumor cell invasion. V-ATPases are large multisubunit complexes, composed of an ATP-hydrolytic domain (V1) and a proton translocation domain (V0), and operate by a rotary mechanism. This review focuses on recent insights into their structure and mechanism, the mechanisms that regulate V-ATPase activity (particularly regulated assembly and trafficking), and the role of V-ATPases in processes such as cell signaling and cancer. These developments have highlighted the potential of V-ATPases as a therapeutic target in a variety of human diseases.

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  • The level of V1 sector association with the V0 sector regulates ATPase and proton pump activities of the vATPase complex on lysosomes.

    “The level of V1 sector association with the V0 sector regulates ATPase and proton pump activities of the vATPase complex on lysosomes (Cotter et al., 2015).”

    From Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99) (2019) · cites this paper as Cotter et al., 2015

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References 115 · Cited by 337

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Authors
Cotter, K., Stransky, L., McGuire, C., & Forgac, M.
Affiliations
Tufts University (US)
Corresponding author
Forgac, Michael
ORCID
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2015-10
Volume
40
Issue
10
Pages
611-622
ISSN
0968-0004 (ISSN-L)
DOI
10.1016/j.tibs.2015.08.005
PMC
PMC4589219
OpenAlex
W2137579115
Cited by
337
References
115
Citations by year
2026: 11 · 2025: 33 · 2024: 34 · 2023: 25 · 2022: 22 · 2021: 52 · 2020: 39 · 2019: 39 · 2018: 35 · 2017: 23 · 2016: 22 · 2015: 1
FWCI
2.62
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Trends in Biochemical Sciences (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Cancer Institute (F31CA192500, F31CA189321)
  • National Institute of General Medical Sciences (R01GM34478, R01GM034478)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
V-ATPase, vacuolar H+-ATPase, proton pump, multisubunit complexes, rotary mechanism, protein trafficking, pH homeostasis, signal transduction, cancer, therapeutic target, membrane trafficking, bone resorption
MeSH terms
Animals, Cell Membrane, Proton-Translocating ATPases, Humans, Structure-Activity Relationship

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