title: Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species.
abstract: 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 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 the different domains of perilipin 3.
authors.affiliation: Departments of Physics, Kent State University, Kent, OH 44242.
authors.forename: Mona
authors.initials: M
authors.lastname: Mirheydari
authors.affiliation: Biological Sciences, Kent State University, Kent, OH 44242.
authors.forename: Sewwandi S
authors.identifier: 0000-0003-4662-8429
authors.initials: SS
authors.lastname: Rathnayake
authors.affiliation: Chemistry and Biochemistry, Kent State University, Kent, OH 44242.
authors.forename: Hannah
authors.initials: H
authors.lastname: Frederick
authors.affiliation: Department of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045.
authors.forename: Taylor
authors.initials: T
authors.lastname: Arhar
authors.affiliation: Departments of Physics, Kent State University, Kent, OH 44242.
authors.forename: Elizabeth K
authors.initials: EK
authors.lastname: Mann
authors.affiliation: Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102.
authors.forename: Simon
authors.initials: S
authors.lastname: Cocklin
authors.affiliation: Biological Sciences, Kent State University, Kent, OH 44242 ekooijma@kent.edu.
authors.forename: Edgar E
authors.initials: EE
authors.lastname: Kooijman
mesh_terms: D006801:Humans; D066292:Lipid Droplets / Q000737:chemistry; D008567:Membranes, Artificial; D000070796:Perilipin-3 / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D021381:Protein Transport; D013816:Thermodynamics
chemical_list: D008567:Membranes, Artificial; D000070796:Perilipin-3; D010743:Phospholipids
keywords: amphipathic alpha-helices; lipid droplets; protein-lipid interaction