Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 60, Issue 6, Pages 1027-1032Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-003-3003-1
Keywords
plasma membrane; microdomain; infection; AIDS; Alzheimer; prion; chaperone; HIV-1; virus fusion; lipid rafts; caveolae
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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).
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