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The protein MOSPD2 MOSPD2 is anchored to the surface of the endoplasmic reticulum and is capable of establishing physical links with lipid droplets, cellular structures that store energy in the form of cholesterol and triglyceride esters. Intriguingly, MOSPD2 possesses a structural domain found in many proteins involved in lipid transport. Our hypothesis is that MOSPD2 transports lipids between the ER and lipid droplets to ensure the biogenesis of these droplets and/or the persistence of these structures over time. We therefore seek to biochemically characterize the MOSPD2 protein to better document the potential role of lipid transfer in lipid droplet biology, an aspect that remains extremely poorly understood – in collaboration with Dr. F. Alpy (IGBMC, Illkirch).

ANR LipDropER

2022
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 AR, Kobayashi T, Drin G, Tomasetto C, Alpy F, MOSPD2 is an endoplasmic reticulum-lipid droplet tether functioning in LD homeostasis. J Cell Biol 2022 Jun; 221(6): .
2018
Di Mattia T, Wilhelm LP, Ikhlef S, Wendling C, Spehner D, Nominé Y, Giordano F, Mathelin C, Drin G, Tomasetto C, Alpy F, Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites. EMBO Rep 2018 Jul; 19(7): .
2020
Di Mattia T, Martinet A, Ikhlef S, McEwen AG, Nominé Y, Wendling C, Poussin-Courmontagne P, Voilquin L, Eberling P, Ruffenach F, Cavarelli J, Slee J, Levine TP, Drin G, Tomasetto C, Alpy F , FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. EMBO J 2020 Dec; 39(23): e104369.