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RESEARCH PRODUCT
Cholesterol trafficking and raft-like membrane domain composition mediate scavenger receptor class B type 1-dependent lipid sensing in intestinal epithelial cells
Armelle LeturqueGé Raldine LucchiVéronique CarrièreSylvie DemignotSara GhezzalEtienne MorelPhilip W. ShaulFrançoise Simon-plasChieko MineoJean-paul Pais De BarrosMonique RoussetCaroline Truntzersubject
0301 basic medicineArticlescavenger receptor03 medical and health scienceschemistry.chemical_compoundMembrane MicrodomainsLipid droplet[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyScavenger receptorIntestinal MucosaMolecular BiologyLipid raft[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyCholesterolcholesterolEpithelial CellsCell BiologyLipid DropletsScavenger Receptors Class BSphingolipidCell biologySphingomyelinslipid raftTransmembrane domain030104 developmental biologychemistrylipid traffickinglipids (amino acids peptides and proteins)sphingolipidSignal transductionCaco-2 CellsLysophospholipidsSphingomyelinSignal Transductiondescription
IF 5.547; International audience; Scavenger receptor Class B type 1 (SR-B1) is a lipid transporter and sensor. In intestinal epithelial cells, SR-B1-dependent lipid sensing is associated with SR-B1 recruitment in raft-like/ detergent-resistant membrane domains and interaction of its C-terminal transmembrane domain with plasma membrane cholesterol. To clarify the initiating events occurring during lipid sensing by SR-B1, we analyzed cholesterol trafficking and raft-like domain composition in intestinal epithelial cells expressing wild-type SR-B1 or the mutated form SR-B1-Q445A, defective in membrane cholesterol binding and signal initiation. These features of SR-B1 were found to influence both apical cholesterol efflux and intracellular cholesterol trafficking from plasma membrane to lipid droplets, and the lipid composition of raft-like domains. Lipidomic analysis revealed likely participation of d18:0/16:0 sphingomyelin and 16:0/0:0 lysophosphatidylethanolamine in lipid sensing by SR-B1. Proteomic analysis identified proteins, whose abundance changed in raft-like domains during lipid sensing, and these included molecules linked to lipid raft dynamics and signal transduction. These findings provide new insights into the role of SR-B1 in cellular cholesterol homeostasis and suggest molecular links between SR-B1-dependent lipid sensing and cell cholesterol and lipid droplet dynamics.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2018-02-01 |