| Literature DB >> 35389430 |
Mehdi Zouiouich1,2,3,4, Thomas Di Mattia1,2,3,4, Arthur Martinet1,2,3,4, Julie Eichler1,2,3,4, Corinne Wendling1,2,3,4, Nario Tomishige5, Erwan Grandgirard1,2,3,4, Nicolas Fuggetta6, Catherine Fromental-Ramain1,2,3,4, Giulia Mizzon7, Calvin Dumesnil8, Maxime Carpentier8, Bernardo Reina-San-Martin1,2,3,4, Carole Mathelin1,2,3,4,9, Yannick Schwab7, Abdou Rachid Thiam8, Toshihide Kobayashi5, Guillaume Drin6, Catherine Tomasetto1,2,3,4, Fabien Alpy1,2,3,4.
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.Entities:
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Year: 2022 PMID： 35389430 PMCID： PMC8996327 DOI： 10.1083/jcb.202110044
Source DB: PubMed Journal: J Cell Biol ISSN： 0021-9525 Impact factor: 10.539