Evidence map›Paper›PMID 25903133›Full record

ArticleThe Journal of biological chemistry2015

Vacuolar ATPase in phagosome-lysosome fusion.

Sandra Kissing, Christina Hermsen, Urska Repnik, Cecilie Kåsi Nesset, Kristine von Bargen, Gareth Griffiths, Atsuhiro Ichihara, Beth S Lee, Michael Schwake, Jef De Brabander and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

56 citing papers in PubMed, 95 citations in OpenAlex.

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  18. ReplicativebioRxiv : the preprint server for biology · 2023
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  19. Frontiers in cellular and infection microbiology · 2023
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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

12 authors at 6 institutions in 4 countries.

Sandra KissingFrom the Institute of Biochemistry, Christian-Albrechts-University of Kiel, D-24098 Kiel, Germany.
Christina HermsenInstitute for Cell Biology, Friedrich-Wilhelms University, D-53121 Bonn, Germany.
Urska RepnikDepartment of Biosciences, University of Oslo, 0316 Oslo, Norway.
Cecilie Kåsi NessetDepartment of Biosciences, University of Oslo, 0316 Oslo, Norway.
Kristine von BargenInstitute for Cell Biology, Friedrich-Wilhelms University, D-53121 Bonn, Germany.
Gareth GriffithsDepartment of Biosciences, University of Oslo, 0316 Oslo, Norway.
Atsuhiro IchiharaDepartment of Medicine II, Tokyo Women's Medical University, Tokyo 162-866, Japan.
Beth S LeeDepartment of Physiology and Cell Biology, The Ohio State University College of Medicine, Columbus, Ohio 42210.
Michael SchwakeDepartment of Chemistry, Biochemistry III, University of Bielefeld, D-33615 Bielefeld, Germany, and.
Jef De BrabanderDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Albert HaasInstitute for Cell Biology, Friedrich-Wilhelms University, D-53121 Bonn, Germany, albert.haas@uni-bonn.de.
Paul SaftigFrom the Institute of Biochemistry, Christian-Albrechts-University of Kiel, D-24098 Kiel, Germany, psaftig@biochem.uni-kiel.de.
University of Bonn · DEUniversity of Oslo · NOKiel University · DEBielefeld University · DEThe University of Texas Southwestern Medical Center · USTokyo Women's Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vacuolar H(+)-ATPase (v-ATPase) complex is instrumental in establishing and maintaining acidification of some cellular compartments, thereby ensuring their functionality. Recently it has been proposed that the transmembrane V0 sector of v-ATPase and its a-subunits promote membrane fusion in the endocytic and exocytic pathways independent of their acidification functions. Here, we tested if such a proton-pumping independent role of v-ATPase also applies to phagosome-lysosome fusion. Surprisingly, endo(lyso)somes in mouse embryonic fibroblasts lacking the V0 a3 subunit of the v-ATPase acidified normally, and endosome and lysosome marker proteins were recruited to phagosomes with similar kinetics in the presence or absence of the a3 subunit. Further experiments used macrophages with a knockdown of v-ATPase accessory protein 2 (ATP6AP2) expression, resulting in a strongly reduced level of the V0 sector of the v-ATPase. However, acidification appeared undisturbed, and fusion between latex bead-containing phagosomes and lysosomes, as analyzed by electron microscopy, was even slightly enhanced, as was killing of non-pathogenic bacteria by V0 mutant macrophages. Pharmacologically neutralized lysosome pH did not affect maturation of phagosomes in mouse embryonic cells or macrophages. Finally, locking the two large parts of the v-ATPase complex together by the drug saliphenylhalamide A did not inhibit in vitro and in cellulo fusion of phagosomes with lysosomes. Hence, our data do not suggest a fusion-promoting role of the v-ATPase in the formation of phagolysosomes.

Indexed as

AnimalsEscherichia coliFemaleFibroblastsHydrogen-Ion ConcentrationLysosomesMacrophagesMaleMembrane FusionMiceMice, KnockoutMice, TransgenicMicroscopy, ElectronMicroscopy, FluorescencePhagosomesProrenin ReceptorATP6AP2 protein, mouseProrenin ReceptorProton-Translocating ATPasesReceptors, Cell SurfaceVacuolar Proton-Translocating ATPasesATP6AP2lysosomal acidificationlysosomemembrane fusionphagocytosisphagosome maturationvacuolar ATPase

Identifiers

PMID25903133
PMCPMC4447986
OpenAlexW1987146298

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.