Reference: Khaddaj R, et al. (2022) The surface of lipid droplets constitutes a barrier for endoplasmic reticulum-resident integral membrane proteins. J Cell Sci 135(5)

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Abstract


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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Khaddaj R, Mari M, Cottier S, Reggiori F, Schneiter R
Primary Lit For
WBP1 | SEC61 | SCS3 | ERG6 | YFT2

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 3 entries for 3 genes

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InteractorInteractorAssayAnnotationActionModification

BiFC

ERG6ERG6PCAmanually curatedHit-BaitNo Modification

BiFC

SEC61ERG6PCAmanually curatedHit-BaitNo Modification

BiFC

WBP1ERG6PCAmanually curatedHit-BaitNo Modification
Showing 1 to 3 of 3 entries