Evidence map›Paper›PMID 24856514›Full record

ArticleDevelopmental cell2014

VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface.

Geoffrey G Hesketh, Inmaculada Pérez-Dorado, Lauren P Jackson, Lena Wartosch, Ingmar B Schäfer, Sally R Gray, Airlie J McCoy, Oliver B Zeldin, Elspeth F Garman, Michael E Harbour and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

79 citing papers in PubMed, 130 citations in OpenAlex.

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  6. Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2025
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19 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

14 authors at 4 institutions in 1 country.

Geoffrey G HeskethCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Inmaculada Pérez-DoradoMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
Lauren P JacksonCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Lena WartoschCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Ingmar B SchäferMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
Sally R GrayCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Airlie J McCoyCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Oliver B ZeldinDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Elspeth F GarmanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Michael E HarbourCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
Philip R EvansMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
Matthew N J SeamanCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK. Electronic address: mnjs100@cam.ac.uk.
J Paul LuzioCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK. Electronic address: jpl10@cam.ac.uk.
David J OwenCambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK. Electronic address: djo30@cam.ac.uk.
Wellcome Trust · GBUniversity of Cambridge · GBMedical Research Council · GBUniversity of Oxford · GB

Funding

CIHRMedical Research Council G0700750Medical Research Council G0701444Medical Research Council G0900113Medical Research Council MC_U105178845Medical Research Council U105178845Wellcome Trust 090909Wellcome Trust 100140Wellcome Trust G0900113
6 · The paper itself

Abstract

VARP is a Rab32/38 effector that also binds to the endosomal/lysosomal R-SNARE VAMP7. VARP binding regulates VAMP7 participation in SNARE complex formation and can therefore influence VAMP7-mediated membrane fusion events. Mutant versions of VARP that cannot bind Rab32:GTP, designed on the basis of the VARP ankyrin repeat/Rab32:GTP complex structure described here, unexpectedly retain endosomal localization, showing that VARP recruitment is not dependent on Rab32 binding. We show that recruitment of VARP to the endosomal membrane is mediated by its direct interaction with VPS29, a subunit of the retromer complex, which is involved in trafficking from endosomes to the TGN and the cell surface. Transport of GLUT1 from endosomes to the cell surface requires VARP, VPS29, and VAMP7 and depends on the direct interaction between VPS29 and VARP. Finally, we propose that endocytic cycling of VAMP7 depends on its interaction with VARP and, consequently, also on retromer.

Indexed as

Amino Acid SequenceBlotting, WesternCell MembraneCrystallography, X-RayEndosomesGlucose Transporter Type 1Guanine Nucleotide Exchange FactorsGuanosine TriphosphateHeLa CellsHumansImmunoprecipitationMolecular Sequence DataMuscle ProteinsMutagenesis, Site-DirectedNuclear ProteinsProtein BindingANKRD1 protein, humanANKRD27 protein, humanGlucose Transporter Type 1Guanine Nucleotide Exchange FactorsGuanosine TriphosphateMuscle ProteinsNuclear ProteinsRab32 protein, humanrab GTP-Binding ProteinsRepressor ProteinsR-SNARE ProteinsSLC2A1 protein, humanVAMP7 protein, humanVesicular Transport ProteinsVPS29 protein, human

Identifiers

PMID24856514
PMCPMC4059916
OpenAlexW2079989614

What OpenQuestion holds

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Read underepoch 390

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.