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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2003 Jun;60(6):1027–1032. doi: 10.1007/s00018-003-3003-1

How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains

J Fantini 1
PMCID: PMC11138889  PMID: 12866532

Abstract:

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).

Keywords: Key words: Plasma membrane; microdomain; infection; AIDS; Alzheimer; prion; chaperone; HIV-1; virus fusion; lipid rafts; caveolae.

Footnotes

Received 8 January 2003; received after revision 27 February 2003; accepted 14 March 2003


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