Fig. 1: Triglyceride precursors DAG and PA recruit PLIN3 to membrane bilayers.

a Structures of representative phospholipids used in this study. The level of lipid packing defects are depicted as gradient color from red (strong) to pale red (weak). b SDS-PAGE analysis of human PLIN3 liposome sedimentation assay using either palmitoyl-oleoyl (PO)-liposomes or di-oleoyl (DO)-liposomes with different ratios of PC to PE (n = 3). Lane S (supernatant) and P (pellet) represent unbound and bound human PLIN3 to liposomes. Lane I represents input of protein. c SDS-PAGE analysis of human PLIN3 recruitment to liposomes enriched with 20 mol% of the additional lipids PS, PA, DAG, PI and ceramide (n = 3). d Quantification of PLIN3 recruitment to liposomes in different lipid compositions. Data are presented as mean values +/− SD from three independent experiments (n = 3). e SDS-PAGE analysis of human PLIN3 recruitment to DO-liposomes using different amounts of DAG. DOPE concentration was held constant at 20 mol% and DOPC was adjusted between 60 and 79 mol% to maintain total phospholipid concentration. Bar graph shows addition of DAG increases PLIN3 binding (n = 2). f SDS-PAGE analysis of human PLIN3 recruitment to DO-liposomes enriched with different amount of DOPA. The amounts of DOPE and DAG were kept constant at 20 mol%. DOPC concentration was adjusted between 40 and 60 mol% to maintain total phospholipid concentration. Bar graph shows addition of DOPA further increases PLIN3 binding. Data are presented as mean values +/− SD (n = 3). g SDS-PAGE analysis of human PLIN3 recruitment to 4ME liposomes enriched with 20 mol% of the additional lipids 4ME-PA, 4ME-PS, ceramide. 4ME-PC and 4ME-PE concentrations ranged between 60–80 mol% and 20 mol%, respectively (n = 2). Lane M represents protein ladder marker. Source data are provided as a Source Data file.