Evidence map›Paper›PMID 26442671›Full record

ArticleScientific reports2015

Mapping the H(+) (V)-ATPase interactome: identification of proteins involved in trafficking, folding, assembly and phosphorylation.

Maria Merkulova, Teodor G Păunescu, Anie Azroyan, Vladimir Marshansky, Sylvie Breton, Dennis Brown

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 8% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 142 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. WDR72 Is Required for Urinary Acidification and Normal HActa physiologica (Oxford, England) · 2026
    Article
  7. Article
  8. ATG16L1 controls mammalian vacuolar proton ATPase.The Journal of cell biology · 2025
    Article
  9. V-ATPase assembly at leaky lysosomes.Nature structural & molecular biology · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Oxr1 and Ncoa7 regulate V-ATPase to achieve optimal pH for glycosylation within the Golgi apparatus and trans-Golgi network.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

28 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

6 authors at 1 institution in 1 country.

Maria MerkulovaMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Teodor G PăunescuMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Anie AzroyanMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Vladimir MarshanskyMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Sylvie BretonMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Dennis BrownMGH Center for Systems Biology, Program in Membrane Biology &Division of Nephrology, Richard B. Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
Center for Systems Biology · US

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI RAYMOND T CHUNG · 1991 to 2026
$35.3M
Transgenic CoreP30DK057521 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI KAHN, BARBARA B. · 2000 to 2019
$31.4M
Transfer of grant 5R01HD040793 - Intercellular networks and luminal acidification in the male reproductive tractR01HD040793 · NICHD · MASSACHUSETTS GENERAL HOSPITAL · PI BRETON, SYLVIE · 2001 to 2021
$6.6M
Regulation of proton pump trafficking in kidneyR37DK042956 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS · 2008 to 2017
$4.0M
CELLULAR REGULATION OF KIDNEY EPITHELIAL CELL POLARITYR01DK042956 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS · 1991 to 2006
$2.2M
pH-sensing and activation of acid secretion by the V-ATPaseR01DK097124 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BRETON, SYLVIE · 2013 to 2016
$1.5M
Regulation of proton pump trafficking in kidneyR56DK042956 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS · 2018 to 2018
$100k
NICHD NIH HHS HD040793NICHD NIH HHS R01 HD040793NIDDK NIH HHS DK042956NIDDK NIH HHS DK097124NIDDK NIH HHS DK43351NIDDK NIH HHS P30 DK043351NIDDK NIH HHS P30 DK057521NIDDK NIH HHS R01 DK042956NIDDK NIH HHS R01 DK097124NIDDK NIH HHS R37 DK042956NIDDK NIH HHS R56 DK042956
6 · The paper itself

Abstract

V-ATPases (H(+) ATPases) are multisubunit, ATP-dependent proton pumps that regulate pH homeostasis in virtually all eukaryotes. They are involved in key cell biological processes including vesicle trafficking, endosomal pH sensing, membrane fusion and intracellular signaling. They also have critical systemic roles in renal acid excretion and blood pH balance, male fertility, bone remodeling, synaptic transmission, olfaction and hearing. Furthermore, V-ATPase dysfunction either results in or aggravates various other diseases, but little is known about the complex protein interactions that regulate these varied V-ATPase functions. Therefore, we performed a proteomic analysis to identify V-ATPase associated proteins and construct a V-ATPase interactome. Our analysis using kidney tissue revealed V-ATPase-associated protein clusters involved in protein quality control, complex assembly and intracellular trafficking. ARHGEF7, DMXL1, EZR, NCOA7, OXR1, RPS6KA3, SNX27 and 9 subunits of the chaperonin containing TCP1 complex (CCT) were found to interact with V-ATPase for the first time in this study. Knockdown of two interacting proteins, DMXL1 and WDR7, inhibited V-ATPase-mediated intracellular vesicle acidification in a kidney cell line, providing validation for the utility of our interactome as a screen for functionally important novel V-ATPase-regulating proteins. Our data, therefore, provide new insights and directions for the analysis of V-ATPase cell biology and (patho)physiology.

Indexed as

Protein Interaction MapsAnimalsImmunoprecipitationMice, Inbred C57BLMice, KnockoutMice, TransgenicNerve Tissue ProteinsPhosphorylationProtein FoldingProtein Interaction MappingProtein TransportVacuolar Proton-Translocating ATPasesAtp6v1b1 protein, mouseDMXL2 protein, mouseNerve Tissue ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID26442671
PMCPMC4595830
OpenAlexW1927156752

What OpenQuestion holds

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Registered trials

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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.