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

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...

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Published inThe Journal of cell biology Vol. 221; no. 6; p. 1
Main Authors 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
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 06.06.2022
Subjects
Cellular Biology
Domains
Droplets
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Homeostasis
Life Sciences
Lipid Droplets - metabolism
Lipids
Membrane proteins
Membrane Proteins - metabolism
Membranes
Mitochondrial Membranes
Organelles
Proteins
Receptors, Chemokine - metabolism
Tethering
Tethers
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Summary: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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PMCID: PMC8996327
ISSN:0021-9525
1540-8140
1540-8140
DOI:10.1083/jcb.202110044