Evidence map›Paper›PMID 35389430›Full record

ArticleThe Journal of cell biology2022

MOSPD2 is an endoplasmic reticulum-lipid droplet tether functioning in LD homeostasis.

Mehdi Zouiouich, Thomas Di Mattia, Arthur Martinet, Julie Eichler, Corinne Wendling, Nario Tomishige, Erwan Grandgirard, Nicolas Fuggetta, Catherine Fromental-Ramain, Giulia Mizzon and 10 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. The evolving landscape of ER-LD contact sites.Frontiers in cell and developmental biology · 2024
    Review
  13. The novel bacterial effector proteinbioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Seipin-still a mysterious protein?Frontiers in cell and developmental biology · 2023
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. CContact (Thousand Oaks (Ventura County, Calif.))
    Review
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

20 authors.

Mehdi ZouiouichIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0003-4333-8792
Thomas Di MattiaIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-9974-7352
Arthur MartinetIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-9286-306X
Julie EichlerIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0003-3990-9986
Corinne WendlingIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.
Nario TomishigeLaboratoire de Bioimagerie et Pathologies, UMR 7021 CNRS, Faculté de Pharmacie, Université de Strasbourg, Illkirch, France.ORCID 0000-0002-1266-5400
Erwan GrandgirardIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-5263-2144
Nicolas FuggettaUniversité Côte d'Azur, Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.ORCID 0000-0002-8508-3188
Catherine Fromental-RamainIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-3573-3154
Giulia MizzonEuropean Molecular Biology Laboratory, Cell Biology and Biophysics Unit, Heidelberg, Germany.ORCID 0000-0001-9392-9748
Calvin DumesnilLaboratoire de Physique de l'École Normale Supérieure, Université Paris Sciences and Lettres, Centre National de la Recherche Scientifique, Sorbonne Université, Université de Paris, Paris, France.
Maxime CarpentierLaboratoire de Physique de l'École Normale Supérieure, Université Paris Sciences and Lettres, Centre National de la Recherche Scientifique, Sorbonne Université, Université de Paris, Paris, France.
Bernardo Reina-San-MartinIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0003-2083-6166
Carole MathelinIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-7680-0210
Yannick SchwabEuropean Molecular Biology Laboratory, Cell Biology and Biophysics Unit, Heidelberg, Germany.ORCID 0000-0001-8027-1836
Abdou Rachid ThiamLaboratoire de Physique de l'École Normale Supérieure, Université Paris Sciences and Lettres, Centre National de la Recherche Scientifique, Sorbonne Université, Université de Paris, Paris, France.ORCID 0000-0001-7488-4724
Toshihide KobayashiLaboratoire de Bioimagerie et Pathologies, UMR 7021 CNRS, Faculté de Pharmacie, Université de Strasbourg, Illkirch, France.ORCID 0000-0002-4811-7270
Guillaume DrinUniversité Côte d'Azur, Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.ORCID 0000-0002-3484-4581
Catherine TomasettoIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-1811-5848
Fabien AlpyIGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.ORCID 0000-0002-0526-0720

Funding

Agence Nationale de la Recherche ANR-21-CE13-0014-01Centre national de la recherche scientifiqueEUR IMCBio ANR-17-EURE-0023Fondation ARC pour la recherche sur le cancerFondation pour la Recherche MédicaleIdEx Unistra ANR-10-IDEX-0002Institut National de la Santé et de la Recherche MédicaleITMO Cancer AVIESANLigue Contre le CancerSFRI-STRAT'US ANR 20-SFRI-0012Université de Strasbourg
6 · The paper itself

Abstract

Membrane contact sites between organelles are organized by protein bridges. Among the components of these contacts, the VAP family comprises ER-anchored proteins, such as MOSPD2, that function as major ER-organelle tethers. MOSPD2 distinguishes itself from the other members of the VAP family by the presence of a CRAL-TRIO domain. In this study, we show that MOSPD2 forms ER-lipid droplet (LD) contacts, thanks to its CRAL-TRIO domain. MOSPD2 ensures the attachment of the ER to LDs through a direct protein-membrane interaction. The attachment mechanism involves an amphipathic helix that has an affinity for lipid packing defects present at the surface of LDs. Remarkably, the absence of MOSPD2 markedly disturbs the assembly of lipid droplets. These data show that MOSPD2, in addition to being a general ER receptor for inter-organelle contacts, possesses an additional tethering activity and is specifically implicated in the biology of LDs via its CRAL-TRIO domain.

Indexed as

Endoplasmic ReticulumLipid DropletsMembrane ProteinsReceptors, ChemokineHomeostasisMitochondrial MembranesMembrane ProteinsReceptors, Chemokine

Identifiers

PMID35389430
PMCPMC8996327

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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.