Schematic representation of ER–LD contact sites mediated by MOSPD2. MOSPD2 tethers the ER to LDs thanks to its TM and CRAL-TRIO domains. The amphipathic helix located in the CRAL-TRIO domain directly interacts with the surface of LDs. The CRAL-TRIO domain of MOSPD2 might also be involved in lipid binding and/or transport between the ER and LDs.