title: Lipid membrane domains in cell surface and vacuolar systems.
abstract: Detergent insoluble sphingolipid-cholesterol enriched 'raft'-like membrane microdomains have been implicated in a variety of biological processes including sorting, trafficking, and signaling. Mutant cells and knockout animals of sphingolipid biosynthesis are clearly useful to understand the biological roles of lipid components in raft-like domains. It is suggested that raft-like domains distribute in internal vacuolar membranes as well as plasma membranes. In addition to sphingolipid-cholesterol-rich membrane domains, recent studies suggest the existence of another lipid-membrane domain in the endocytic pathway. This domain is enriched with a unique phospholipid, lysobisphosphatidic acid (LBPA) and localized in the internal membrane of multivesicular endosome. LBPA-rich membrane domains are involved in lipid and protein sorting within the endosomal system. Possible interaction between sphingolipids and LBPA in sphingolipid-storage disease is discussed.
authors.affiliation: Supra-Biomolecular System Research Group, Frontier Research System, The Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama, Japan. kobayasi@postman.riken.go.jp
authors.forename: T
authors.initials: T
authors.lastname: Kobayashi
authors.forename: Y
authors.initials: Y
authors.lastname: Hirabayashi
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D018432:Drug Resistance, Multiple; D011992:Endosomes / Q000378:metabolism; D005963:Glucosylceramides / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D006801:Humans; D008563:Membrane Lipids / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D013107:Sphingolipids / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism*
chemical_list: D005963:Glucosylceramides; D008563:Membrane Lipids; D013107:Sphingolipids