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MOSPD2 is an endoplasmic reticulum–lipid droplet tether functioning in LD homeostasis
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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.
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Metadata
- Authors
- Zouiouich, M., Di Mattia, T., Martinet, A., Eichler, J., Wendling, C., Tomishige, N., Grandgirard, E., Fuggetta, N., Fromental-Ramain, C., Mizzon, G., Dumesnil, C., Carpentier, M., Reina-San-Martin, B., Mathelin, C., Schwab, Y., Thiam, A. R., Kobayashi, T., Drin, G., Tomasetto, C., & Alpy, F.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- IGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France 1
- European Molecular Biology Laboratory (DE)
- Corresponding author
- Tomasetto, Catherine
- Alpy, Fabien
- ORCID
- Zouiouich, Mehdi
- Di Mattia, Thomas
- Martinet, Arthur
- Eichler, Julie
- Wendling, Corinne
- Tomishige, Nario
- Grandgirard, Erwan
- Fuggetta, Nicolas
- Fromental-Ramain, Catherine
- Mizzon, Giulia
- Dumesnil, Calvin
- Carpentier, Maxime
- Reina-San-Martin, Bernardo
- Mathelin, Carole
- Schwab, Yannick
- Thiam, Abdou Rachid
- Kobayashi, Toshihide
- Drin, Guillaume
- Tomasetto, Catherine
- Alpy, Fabien
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2022-04-07
- Volume
- 221
- Issue
- 6
- Pages
- e202110044
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC8996327
- OpenAlex
- W4224073523
- Cited by
- 40
- References
- 65
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 8 · 2023: 7 · 2022: 5
- FWCI
- 3.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion, other-oa)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by-nc-sa)
- Funders
- Agence Nationale de la Recherche (ANR-21-CE13-0014-01, ANR-19-CE44-0003)
- Ligue Contre le Cancer
- Université de Strasbourg
- Institut National de la Santé et de la Recherche Médicale
- SFRI-STRAT’US (ANR 20-SFRI-0012)
- EUR IMCBio (ANR-17-EURE-0023)
- IdEx Unistra (ANR-10-IDEX-0002)
- ITMO Cancer AVIESAN
- Fondation pour la Recherche Médicale
- Fondation ARC pour la recherche sur le cancer
- Centre national de la recherche scientifique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- VAP proteins, endoplasmic reticulum, lipid droplets, membrane contact sites, lipid droplet homeostasis, amphipathic helix, lipid packing defects, protein-membrane interactions
- MeSH terms
- Endoplasmic Reticulum, Homeostasis, Membrane Proteins, Receptors, Chemokine, Mitochondrial Membranes, Lipid Droplets
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