Surface tension-driven sorting of human perilipins on lipid droplets.

Autor:	Dias Araújo AR; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Bello AA; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Bigay J; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Franckhauser C; Centre de Recherche en Biologie Cellulaire de Montpellier-CRBM, Université de Montpellier, CNRS, UMR 5237 , Montpellier, France., Gautier R; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Cazareth J; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Kovács D; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Brau F; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France., Fuggetta N; Centre de Recherche en Biologie Cellulaire de Montpellier-CRBM, Université de Montpellier, CNRS, UMR 5237 , Montpellier, France., Čopič A; Centre de Recherche en Biologie Cellulaire de Montpellier-CRBM, Université de Montpellier, CNRS, UMR 5237 , Montpellier, France., Antonny B; Université Côte d'Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 , Sophia Antipolis, France.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2024 Dec 02; Vol. 223 (12). Date of Electronic Publication: 2024 Sep 19.
DOI:	10.1083/jcb.202403064
Abstrakt:	Perilipins (PLINs), the most abundant proteins on lipid droplets (LDs), display similar domain organization including amphipathic helices (AH). However, the five human PLINs bind different LDs, suggesting different modes of interaction. We established a minimal system whereby artificial LDs covered with defined polar lipids were transiently deformed to promote surface tension. Binding of purified PLIN3 and PLIN4 AH was strongly facilitated by tension but was poorly sensitive to phospholipid composition and to the presence of diacylglycerol. Accordingly, LD coverage by PLIN3 increased as phospholipid coverage decreased. In contrast, PLIN1 bound readily to LDs fully covered by phospholipids; PLIN2 showed an intermediate behavior between PLIN1 and PLIN3. In human adipocytes, PLIN3/4 were found in a soluble pool and relocated to LDs upon stimulation of fast triglyceride synthesis, whereas PLIN1 and PLIN2 localized to pre-existing LDs, consistent with the large difference in LD avidity observed in vitro. We conclude that the PLIN repertoire is adapted to handling LDs with different surface properties. (© 2024 Dias Araujo et al.)
Databáze:	MEDLINE
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