How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains.
Understanding the molecular mechanisms controlling the association of proteins with lipid rafts is a central issue in cell biology and medicine. A structurally conserved motif (the 'sphingolipid binding domain') has been characterized in unrelated cellular and microbial proteins targeted to lipid rafts. I propose that the structuration of a sphingolipid shell around the sphingolipid binding domain not only extracts the protein from the liquid-disordered phase of the plasma membrane, and ensures its delivery to lipid rafts, but also influences its conformation. The chaperone activity of sphingolipids in shells and rafts may play an important role in infectious and conformational diseases(human immunodeficiency virus-1, prions, Alzheimer).
Fantini
J
J
Laboratoire de Biochimie et Physicochemie des Membranes Biologiques, Institut Méditerranéen de Recherche en nutrition, UMR-INRA 1111, Faculté des Sciences de St-Jêrome, Marseille, France. jacques.fantini@univ.u-3mrs.fr
D000544:Alzheimer Disease / Q000378:metabolism; D001665:Binding Sites; D015658:HIV Infections / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D021962:Membrane Microdomains / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D013107:Sphingolipids / Q000737:chemistry* / Q000378:metabolism*
D008565:Membrane Proteins; D018832:Molecular Chaperones; D013107:Sphingolipids