Evidence map›Paper›PMID 29858488›Full record

ArticleEMBO reports2018

Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites.

Thomas Di Mattia, Léa P Wilhelm, Souade Ikhlef, Corinne Wendling, Danièle Spehner, Yves Nominé, Francesca Giordano, Carole Mathelin, Guillaume Drin, Catherine Tomasetto and 1 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 2% 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, 1 synthesis or guideline pooled it, 130 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
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  3. Review
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  9. Mitochondria-ER crosstalk via MAMS: Bridging cellular homeostasis and cancer progression.Apoptosis : an international journal on programmed cell death · 2026
    Review
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  18. Article
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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

11 authors at 1 institution in 1 country.

Thomas Di MattiaInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.ORCID 0000-0002-9974-7352
Léa P WilhelmInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.ORCID 0000-0001-5926-4666
Souade IkhlefCNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Valbonne, France.
Corinne WendlingInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
Danièle SpehnerInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
Yves NominéInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
Francesca GiordanoInstitut de Biologie Intégrative de la Cellule, CEA, CNRS, Paris-Sud University Paris-Saclay University, Gif-sur-Yvette Cedex 91198, France.ORCID 0000-0002-5942-1753
Carole MathelinInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
Guillaume DrinCNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Valbonne, France.
Catherine TomasettoInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France catherine-laure.tomasetto@igbmc.fr fabien.alpy@igbmc.fr.ORCID 0000-0002-1811-5848
Fabien AlpyInstitut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France catherine-laure.tomasetto@igbmc.fr fabien.alpy@igbmc.fr.ORCID 0000-0002-0526-0720
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane contact sites are cellular structures that mediate interorganelle exchange and communication. The two major tether proteins of the endoplasmic reticulum (ER), VAP-A and VAP-B, interact with proteins from other organelles that possess a small VAP-interacting motif, named FFAT [two phenylalanines (FF) in an acidic track (AT)]. In this study, using an unbiased proteomic approach, we identify a novel ER tether named motile sperm domain-containing protein 2 (MOSPD2). We show that MOSPD2 possesses a Major Sperm Protein (MSP) domain which binds FFAT motifs and consequently allows membrane tethering

Indexed as

Amino Acid MotifsAnimalsBinding SitesEndoplasmic ReticulumEndosomesGolgi ApparatusHumansMaleMembrane ProteinsMiceMitochondrial MembranesProtein BindingProteomicsReceptors, ChemokineSpermatozoaVesicular Transport ProteinsMembrane ProteinsMOSPD2 protein, humanReceptors, ChemokineVAPA protein, humanVAPB protein, humanVesicular Transport Proteinsendoplasmic reticulumER–organelle contactFFAT motifmembrane contact siteVAP proteins

Identifiers

PMID29858488
PMCPMC6030701
OpenAlexW2806366302

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.