Journal
JOURNAL OF CELL SCIENCE
Volume 135, Issue 5, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.256206
Keywords
Lipid droplets; Endoplasmic reticulum; Saccharomyces cerevisiae; Perilipins; Seipin; Triacylglycerols; Steryl esters
Categories
Funding
- ZonMw TOP [91217002]
- Aard-en Levenswetenschappen
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (ALW) Open Programme [ALWOP.310]
- H2020 Marie Sklodowska-Curie Actions Cofund [713660]
- Marie Sklodowska Curie ETN [765912]
- ALW Open Programme grant [ALWOP.355]
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung [31003A_173003]
- Novartis Stiftung fur Medizinisch-Biologische Forschung [19B140]
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This study investigates the localization of integral membrane proteins to the surface of lipid droplets (LDs) and confirms that the ER-LD junction acts as a barrier for ER-resident integral membrane proteins. The study also reveals that certain membrane proteins can be targeted to LDs through LD-targeted proteins.
Lipid droplets (LDs) are globular subcellular structures that store neutral lipids. LDs are closely associated with the endoplasmic reticulum (ER) and are limited by a phospholipid monolayer harboring a specific set of proteins. Most of these proteins associate with LDs through either an amphipathic helix or a membrane-embedded hairpin motif. Here, we address the question of whether integral membrane proteins can localize to the surface of LDs. To test this, we fused perilipin 3 (PLIN3), a mammalian LD-targeted protein, to ER-resident proteins. The resulting fusion proteins localized to the periphery of LDs in both yeast and mammalian cells. This peripheral LD localization of the fusion proteins, however, was due to a redistribution of the ER around LDs, as revealed by bimolecular fluorescence complementation between ER- and LD-localized partners. A LD-tethering function of PLIN3-containing membrane proteins was confirmed by fusing PLIN3 to the cytoplasmic domain of an outer mitochondrial membrane protein, OM14. Expression of OM14-PLIN3 induced a close apposition between LDs and mitochondria. These data indicate that the ER-LD junction constitutes a barrier for ER-resident integral membrane proteins. This article has an associated First Person interview with the first author of the paper.
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