A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets

Alenka Čopič (), Sandra Antoine-Bally, Manuel Giménez-Andrés, César Torre Garay, Bruno Antonny, Marco M. Manni, Sophie Pagnotta, Jeanne Guihot and Catherine L. Jackson
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Alenka Čopič: Université Paris Diderot, Sorbonne Paris Cité
Sandra Antoine-Bally: Université Paris Diderot, Sorbonne Paris Cité
Manuel Giménez-Andrés: Université Paris Diderot, Sorbonne Paris Cité
César Torre Garay: Université Paris Diderot, Sorbonne Paris Cité
Bruno Antonny: Université Côte d’Azur, CNRS, IPMC
Marco M. Manni: Université Côte d’Azur, CNRS, IPMC
Sophie Pagnotta: Université Côte d’Azur, CNRS, IPMC
Jeanne Guihot: Université Paris Diderot, Sorbonne Paris Cité
Catherine L. Jackson: Université Paris Diderot, Sorbonne Paris Cité

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: Abstract How proteins are targeted to lipid droplets (LDs) and distinguish the LD surface from the surfaces of other organelles is poorly understood, but many contain predicted amphipathic helices (AHs) that are involved in targeting. We have focused on human perilipin 4 (Plin4), which contains an AH that is exceptional in terms of length and repetitiveness. Using model cellular systems, we show that AH length, hydrophobicity, and charge are important for AH targeting to LDs and that these properties can compensate for one another, albeit at a loss of targeting specificity. Using synthetic lipids, we show that purified Plin4 AH binds poorly to lipid bilayers but strongly interacts with pure triglycerides, acting as a coat and forming small oil droplets. Because Plin4 overexpression alleviates LD instability under conditions where their coverage by phospholipids is limiting, we propose that the Plin4 AH replaces the LD lipid monolayer, for example during LD growth.

Date: 2018
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DOI: 10.1038/s41467-018-03717-8

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