Cholesterol trafficking and raft-like membrane domain composition mediate scavenger receptor class B type 1-dependent lipid sensing in intestinal epithelial cells期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

按检索

Cholesterol trafficking and raft-like membrane domain composition mediate scavenger receptor class B type 1-dependent lipid sensing in intestinal epithelial cells

Authors:	Etienne Morel Sara Ghezzal Géraldine Lucchi Caroline Truntzer Jean-Paul Pais de Barros Françoise Simon-Plas Sylvie Demignot Chieko Mineo Philip W Shaul Armelle Leturque Monique Rousset Véronique Carrière

Institution:	1. Centre de Recherche des Cordeliers, INSERM, UMPC Université Paris 6, Université Paris Descartes Paris 5, CNRS, F-75006 Paris, France;2. Clinical Innovation Proteomic Platform CLIPP, Université Bourgogne Franche-Comté, F-21000 Dijon, France;3. Plateforme de Lipidomique, INSERM UMR1231, Université de Bourgogne Franche Comté, F-21000 Dijon, France;4. Agroécologie, AgroSup Dijon, CNRS, INRA, Université Bourgogne Franche-Comté, F-21000 Dijon, France;5. EPHE, PSL Research University, F-75006 Paris, France;6. Center for Pulmonary and Vascular Biology, Department of Pediatrics, University of Texas, Southwestern Medical Center, Dallas, TX, 75390, USA

Abstract:	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.

Keywords:	AGR2 anterior gradient protein 2 homolog CALX calnexin CTTM C-terminal transmembrane domain DRM detergent-resistant membranes HDL high density lipoprotein HNRH1 heterogeneous nuclear ribonucleoprotein H HNRPK heterogeneous nuclear ribonucleoprotein K ICAM1 intercellular adhesion molecule 1 JAM1 junctional adhesion molecule A K1C9 keratin type I cytoskeletal 9 KAP2 cAMP-dependent protein kinase type II-alpha regulatory subunit LDHB L-lactate dehydrogenase B chain LPC lysophosphatidylcholine LPE lysophosphatidylethanolamine MβCD methyl- β-cyclodextrin NDUA2 NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 2 PC phosphatidylcholine PDE8A high affinity cAMP-specific and IBMX-insensitive 3′ 5′-cyclic phosphodiesterase 8A PE phosphatidylethanolamine PI phosphoinositide PL phospholipids pPE plasmalogen phosphatidylethanolamine PPM postprandial lipid micelles PS phosphatidylserine SM sphingomyelin SR-B1 scavenger receptor Class B type 1 STX16 syntaxin-16 VAMP8 vesicle-associated membrane protein 8 VATD ion transport such as V-type proton ATPase subunit D VP9D1 VPS9 domain-containing protein 1 Scavenger receptor Cholesterol Lipid raft Sphingolipid Lipid trafficking
本文献已被 ScienceDirect 等数据库收录！

设为首页 | 免责声明 | 关于勤云 | 加入收藏