Evidence map›Paper›PMID 34103503›Full record

ArticleNature communications2021

Nanoscale architecture of a VAP-A-OSBP tethering complex at membrane contact sites.

Eugenio de la Mora, Manuela Dezi, Aurélie Di Cicco, Joëlle Bigay, Romain Gautier, John Manzi, Joël Polidori, Daniel Castaño-Díez, Bruno Mesmin, Bruno Antonny and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  9. Molecular regulation of calcium-sensing receptor (CaSR)-mediated signaling.Chronic diseases and translational medicine · 2024
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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

11 authors at 2 institutions in 2 countries.

Eugenio de la Mora *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.
Manuela Dezi *Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France. manuela.dezi@curie.fr.ORCID http://orcid.org/0000-0001-8727-9910
Aurélie Di CiccoLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.
Joëlle BigayCNRS UMR 7275, Université Côte d'Azur, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.ORCID http://orcid.org/0000-0002-7487-3416
Romain GautierCNRS UMR 7275, Université Côte d'Azur, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.ORCID http://orcid.org/0000-0001-6678-132X
John ManziLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France.ORCID http://orcid.org/0000-0003-2574-4260
Joël PolidoriCNRS UMR 7275, Université Côte d'Azur, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Daniel Castaño-DíezBioEM Lab, C-CINA, Biozentrum, University of Basel, Basel, Switzerland.
Bruno MesminCNRS UMR 7275, Université Côte d'Azur, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.ORCID http://orcid.org/0000-0002-5437-3246
Bruno AntonnyCNRS UMR 7275, Université Côte d'Azur, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. bruno.antonny@ipmc.cnrs.fr.ORCID http://orcid.org/0000-0002-9166-8668
Daniel LévyLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, Paris, France. daniel.levy@curie.fr.ORCID http://orcid.org/0000-0002-8949-4072
Centre National de la Recherche Scientifique · FRUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane contact sites (MCS) are subcellular regions where two organelles appose their membranes to exchange small molecules, including lipids. Structural information on how proteins form MCS is scarce. We designed an in vitro MCS with two membranes and a pair of tethering proteins suitable for cryo-tomography analysis. It includes VAP-A, an ER transmembrane protein interacting with a myriad of cytosolic proteins, and oxysterol-binding protein (OSBP), a lipid transfer protein that transports cholesterol from the ER to the trans Golgi network. We show that VAP-A is a highly flexible protein, allowing formation of MCS of variable intermembrane distance. The tethering part of OSBP contains a central, dimeric, and helical T-shape region. We propose that the molecular flexibility of VAP-A enables the recruitment of partners of different sizes within MCS of adjustable thickness, whereas the T geometry of the OSBP dimer facilitates the movement of the two lipid-transfer domains between membranes.

Identifiers

PMID34103503
PMCPMC8187361
OpenAlexW3171462395

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.