Evidence map›Paper›PMID 23104059›Full record

ArticleNature structural & molecular biology2012

The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation.

Ingmar B Schäfer, Geoffrey G Hesketh, Nicholas A Bright, Sally R Gray, Paul R Pryor, Philip R Evans, J Paul Luzio, David J Owen

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
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

41 citing papers in PubMed, 79 citations in OpenAlex.

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  14. Melanosome Biogenesis in the Pigmentation of Mammalian Skin.Integrative and comparative biology · 2021
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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

8 authors at 4 institutions in 2 countries.

Ingmar B SchäferMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Geoffrey G Hesketh
Nicholas A Bright
Sally R Gray
Paul R Pryor
Philip R Evans
J Paul Luzio
David J Owen
University of Cambridge · GBMedical Research Council · GBMRC Laboratory of Molecular Biology · GBUniversity of York · GB

Funding

CIHRMedical Research Council G0900113Medical Research Council MC_U105178845Medical Research Council U105178845Wellcome Trust 079895Wellcome Trust 090909
6 · The paper itself

Abstract

SNAREs provide energy and specificity to membrane fusion events. Fusogenic trans-SNARE complexes are assembled from glutamine-contributing SNAREs (Q-SNAREs) embedded in one membrane and an arginine-contributing SNARE (R-SNARE) embedded in the other. Regulation of membrane fusion events is crucial for intracellular trafficking. We identify the endosomal protein Varp as an R-SNARE-binding regulator of SNARE complex formation. Varp colocalizes with and binds to VAMP7, an R-SNARE that is involved in both endocytic and secretory pathways. We present the structure of the second ankyrin repeat domain of mammalian Varp in complex with the cytosolic portion of VAMP7. The VAMP7-SNARE motif is trapped between Varp and the VAMP7 longin domain, and hence Varp kinetically inhibits the ability of VAMP7 to form SNARE complexes. This inhibition will be increased when Varp can also bind to other proteins present on the same membrane as VAMP7, such as Rab32-GTP.

Indexed as

Electrophoresis, Polyacrylamide GelEndocytosisGuanine Nucleotide Exchange FactorsHumansKineticsProtein ConformationR-SNARE ProteinsANKRD27 protein, humanGuanine Nucleotide Exchange FactorsR-SNARE ProteinsVAMP7 protein, human

Identifiers

PMID23104059
PMCPMC3605791
OpenAlexW2046231980

What OpenQuestion holds

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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.