Evidence map›Paper›PMID 16537461›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands.

Petra Dames, Bernhard Zimmermann, Ruth Schmidt, Julia Rein, Martin Voss, Bettina Schewe, Bernd Walz, Otto Baumann

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. The V-type HProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  4. The HAmerican journal of physiology. Cell physiology · 2021
    Review
  5. Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Deletion of the pH sensor GPR4 decreases renal acid excretion.Journal of the American Society of Nephrology : JASN · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. Vacuolar-type proton pumps in insect epithelia.The Journal of experimental biology · 2009
    Review
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

8 authors at 2 institutions in 1 country.

Petra DamesInstitut für Biochemie und Biologie, Universität Potsdam, D-14415 Potsdam, Germany.
Bernhard Zimmermann
Ruth Schmidt
Julia Rein
Martin Voss
Bettina Schewe
Bernd Walz
Otto Baumann
University of Potsdam · DECarl Zeiss (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible assembly of the V0V1 holoenzyme from V0 and V1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. In the blowfly (Calliphora vicina) salivary gland, V-ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the cAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity. Fluorescence measurements of pH changes at the luminal surface of isolated glands demonstrate that cAMP, Sp-adenosine-3',5'-cyclic monophosphorothioate, or forskolin, similar to serotonin, cause V-ATPase-dependent luminal acidification. In addition, V-ATPase-dependent ATP hydrolysis increases upon treatment with these agents. Immunofluorescence microscopy and pelleting assays have demonstrated further that V1 components become translocated from the cytoplasm to the apical membrane and V-ATPase holoenzymes are assembled at the apical membrane during conditions that increase intracellular cAMP. Because these actions occur without a change in cytosolic Ca2+, our findings suggest that the cAMP pathway mediates the reversible assembly and activation of V-ATPase molecules at the apical membrane upon hormonal stimulus.

Indexed as

AnimalsCalciumColforsinCyclic AMPCytosolDipteraHydrogen-Ion ConcentrationIn Vitro TechniquesMultiprotein ComplexesProtein Structure, TertiaryReceptors, SerotoninSalivary GlandsSecond Messenger SystemsVacuolar Proton-Translocating ATPasesCalciumColforsinCyclic AMPMultiprotein ComplexesReceptors, SerotoninVacuolar Proton-Translocating ATPases

Identifiers

PMID16537461
PMCPMC1450166
OpenAlexW1994633155

What OpenQuestion holds

Textmetadata
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.