NR AOFT
AU Fantini,J.
TI How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains.
QU Cellular and Molecular Life Science 2003 Jun; 60(6): 1027-32
PT journal article
AB 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).
ZR 53
MH Alzheimer Disease/metabolism; Binding Sites; HIV Infections/metabolism; Human; In Vitro; Membrane Microdomains/*chemistry/*metabolism; Membrane Proteins/*chemistry/*metabolism; Models, Molecular; Molecular Chaperones/chemistry/metabolism; Protein Binding; Sphingolipids/*chemistry/*metabolism
AD Laboratoire de Biochimie et Physicochemie des Membranes Biologiques, Institut Mediterraneen de Recherche en nutrition, UMR-INRA 1111, Faculte des Sciences de St-Jerome, Marseille, France. jacques.fantini@univ.u-3mrs.fr
SP englisch
PO Schweiz