GPI‐anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida

FEBS Letters

Field, Mark C¹  Smith, Deborah F¹  Denny, Paul W¹ 

[1] Wellcome Trust Laboratories for Molecular Parasitology, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 1AZ, UK

关键词: Lipid raft;    Kinetoplastida;    Glycosylphosphatidylinositol anchor;    Sphingolipid;    Sterol;    GPI;    glycosylphosphatidylinositol;    DRM;    detergent-resistant membrane;    VSG;    variant surface glycoprotein;    LPG;    lipophosphoglycan;    GIPL;    glycoinositol phospholipid;    HASP;    hydrophilic acylated surface protein;    PI;    phosphatidylinositol;    IPC;    inositol phosphorylceramide;    PIP;    phosphatidylinositol phosphate;   

DOI  :  10.1016/S0014-5793(01)02172-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The plasma membranes of the divergent eukaryotic parasites, Leishmania and Trypanosoma, are highly specialised, with a thick coat of glycoconjugates and glycoproteins playing a central role in virulence. Unusually, the majority of these surface macro-molecules are attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor. In mammalian cells and yeast, many GPI-anchored molecules associate with sphingolipid and cholesterol-rich detergent-resistant membranes, known as lipid rafts. Here we show that GPI-anchored parasite macro-molecules (but not the dual acylated Leishmania surface protein (hydrophilic acylated surface protein) or a subset of the GPI-anchored glycoinositol phospholipid glycolipids) are enriched in a sphingolipid/sterol-rich fraction resistant to cold detergent extraction. This observation is consistent with the presence of functional lipid rafts in these ancient, highly polarised organisms.

【 授权许可】

Unknown