Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species[S]

Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species[S]

Blog Article

Lipid droplets (LDs) are organelles that contribute to various cellular functions that are vital for life.Aside from acting as a neutral lipid storage depot, they are also involved in building new membranes, synthesis of steroid hormones, and cell signaling.Many aspects of LD structure and function are not yet well-understood.Here we investigate the interaction of perilipin 3, a member of the perilipin family of LD binding proteins, and three N-terminal truncation mutants with lipid monolayers.

The interaction is studied as Girls Jackets a function of surface pressure for a series of systematically chosen lipids.We find that the C terminus of perilipin 3 has different insertion behavior from that of the longer truncation mutants and the full-length protein.Inclusion of N-terminal sequences with the C terminus decreases the ability of the protein construct to insert in lipid monolayers.Coupling of anionic lipids to negative spontaneous curvature facilitates protein interaction and insertion.

The C terminus shows strong preference for lipids with more saturated fatty acids.This work sheds light on the LD binding properties and function of Cable Covers the different domains of perilipin 3.