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Journal article
Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species
Journal of lipid research, v 57(8), pp 1465-1476
01 Aug 2016
PMID: 27256689
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.(jlr) This work sheds light on the LD binding properties and function of the different domains of perilipin 3.-Mirheydari, M., S. S. Rathnayake, H. Frederick, T. Arhar, E. K. Mann, S. Cocklin, and E. E. Kooijman. Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species.
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Details
- Title
- Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species
- Creators
- Mona Mirheydari - Kent State UniversitySewwandi S. Rathnayake - Kent State UniversityHannah Frederick - Kent State UniversityTaylor Arhar - Loyola Marymount UniversityElizabeth K. Mann - Kent State UniversitySimon Cocklin - Drexel UniversityEdgar E. Kooijman - Kent State University
- Publication Details
- Journal of lipid research, v 57(8), pp 1465-1476
- Publisher
- Elsevier
- Number of pages
- 12
- Grant note
- Kent State University Farris Family Fellowship Ohio Board of Regents CHE-1263087 / National Science Foundation for the NSF-REU Program
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000380752300014
- Scopus ID
- 2-s2.0-84982701955
- Other Identifier
- 991019167540804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology