Evidence map›Paper›PMID 22044153›Full record

ReviewCurrent protein & peptide science2012

Targeting reversible disassembly as a mechanism of controlling V-ATPase activity.

Patricia M Kane

Open access · greenAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
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  4. Review
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  11. Article
  12. Inducing indigestion in malaria parasites: Genetic manipulations of a proton pump.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. The V-ATPaseInternational journal of molecular sciences · 2021
    Review
  20. iScience · 2021
    Article

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Patricia M KaneDept. of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams St., Syracuse, NY 13210, USA. kanepm@upstate.edu
SUNY Upstate Medical University · US

Funding

SUBUNIT STRUCTURE/FUNCTION IN VACUOLAR H+ ATPASESR01GM050322 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KANE, PATRICIA M · 1994 to 2015
$4.1M
NIGMS NIH HHS R01 GM050322NIGMS NIH HHS R01 GM50322
6 · The paper itself

Abstract

Vacuolar proton-translocating ATPases (V-ATPases) are highly conserved proton pumps consisting of a peripheral membrane subcomplex called V1, which contains the sites of ATP hydrolysis, attached to an integral membrane subcomplex called Vo, which encompasses the proton pore. V-ATPase regulation by reversible dissociation, characterized by release of assembled V1 sectors into the cytosol and inhibition of both ATPase and proton transport activities, was first identified in tobacco hornworm and yeast. It has since become clear that modulation of V-ATPase assembly level is also a regulatory mechanism in mammalian cells. In this review, the implications of reversible disassembly for V-ATPase structure are discussed, along with insights into underlying subunit-subunit interactions provided by recent structural work. Although initial experiments focused on glucose deprivation as a trigger for disassembly, it is now clear that V-ATPase assembly can be regulated by other extracellular conditions. Consistent with a complex, integrated response to extracellular signals, a number of different regulatory proteins, including RAVE/rabconnectin, aldolase and other glycolytic enzymes, and protein kinase A have been suggested to control V-ATPase assembly and disassembly. It is likely that multiple signaling pathways dictate the ultimate level of assembly and activity. Tissue-specific V-ATPase inhibition is a potential therapy for osteoporosis and cancer; the possibility of exploiting reversible disassembly in design of novel V-ATPase inhibitors is discussed.

Indexed as

Adenosine TriphosphateAnimalsEnzyme ActivationHumansModels, MolecularProtein ConformationProtein SubunitsVacuolar Proton-Translocating ATPasesAdenosine TriphosphateProtein SubunitsVacuolar Proton-Translocating ATPases

Identifiers

PMID22044153
PMCPMC3536023
OpenAlexW2028638550

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.