Evidence map›Paper›PMID 24578385›Full record

ArticleMolecular & cellular proteomics : MCP2014

The Vac14-interaction network is linked to regulators of the endolysosomal and autophagic pathway.

Ulf Schulze, Beate Vollenbröker, Daniela A Braun, Truc Van Le, Daniel Granado, Joachim Kremerskothen, Benjamin Fränzel, Rafael Klosowski, Johannes Barth, Christian Fufezan and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 62 citations in OpenAlex.

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  18. Insights into Lysosomal PI(3,5)PMolecular cell · 2020
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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

13 authors at 3 institutions in 1 country.

Ulf SchulzeFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Beate VollenbrökerFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Daniela A BraunFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Truc Van LeFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Daniel GranadoFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Joachim KremerskothenFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany;
Benjamin Fränzel‖Analytical Chemistry NC4/72, Biomolecular Mass Spectrometry/Proteincenter, Ruhr-University Bochum, Universitätsstr. 150, D-44801 Bochum, Germany;
Rafael Klosowski‖Analytical Chemistry NC4/72, Biomolecular Mass Spectrometry/Proteincenter, Ruhr-University Bochum, Universitätsstr. 150, D-44801 Bochum, Germany;
Johannes Barth‡‡Institute of Plant Biology and Biotechnology, University of Muenster, Schlossplatz 8, D-48143 Muenster, Germany.
Christian Fufezan‡‡Institute of Plant Biology and Biotechnology, University of Muenster, Schlossplatz 8, D-48143 Muenster, Germany.
Dirk A Wolters‖Analytical Chemistry NC4/72, Biomolecular Mass Spectrometry/Proteincenter, Ruhr-University Bochum, Universitätsstr. 150, D-44801 Bochum, Germany;
Hermann PavenstädtFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany; Hermann.Pavenstaedt@ukmuenster.de weidet@uni-muenster.de.
Thomas WeideFrom the ‡Department of Internal Medicine D, Molecular Nephrology, University Hospital of Muenster, Albert-Schweitzer Campus 1, A14, D-48149 Muenster, Germany; Hermann.Pavenstaedt@ukmuenster.de weidet@uni-muenster.de.
University Hospital Münster · DERuhr University Bochum · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The scaffold protein Vac14 acts in a complex with the lipid kinase PIKfyve and its counteracting phosphatase FIG4, regulating the interconversion of phosphatidylinositol-3-phosphate to phosphatidylinositol-3,5-bisphosphate. Dysfunctional Vac14 mutants, a deficiency of one of the Vac14 complex components, or inhibition of PIKfyve enzymatic activity results in the formation of large vacuoles in cells. How these vacuoles are generated and which processes are involved are only poorly understood. Here we show that ectopic overexpression of wild-type Vac14 as well as of the PIKfyve-binding deficient Vac14 L156R mutant causes vacuoles. Vac14-dependent vacuoles and PIKfyve inhibitor-dependent vacuoles resulted in elevated levels of late endosomal, lysosomal, and autophagy-associated proteins. However, only late endosomal marker proteins were bound to the membranes of these enlarged vacuoles. In order to decipher the linkage between the Vac14 complex and regulators of the endolysosomal pathway, a protein affinity approach combined with multidimensional protein identification technology was conducted, and novel molecular links were unraveled. We found and verified the interaction of Rab9 and the Rab7 GAP TBC1D15 with Vac14. The identified Rab-related interaction partners support the theory that the regulation of vesicular transport processes and phosphatidylinositol-modifying enzymes are tightly interconnected.

Indexed as

AutophagyEndosomesFlavoproteinsGene Expression RegulationHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsLysosomesMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphoric Monoester HydrolasesProtein Interaction MapsProteomicsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSignal TransductionFIG4 protein, humanFlavoproteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphoric Monoester HydrolasesPIKFYVE protein, humanrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanRAB9A protein, humanrab GTP-Binding ProteinsVAC14 protein, human

Identifiers

PMID24578385
PMCPMC4047462
OpenAlexW2136820732

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.