Fantini 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.
Cell Mol Life Sci. 2003 Jun;60(6):1027-32. doi: 10.1007/s00018-003-3003-1.
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).
了解控制蛋白质与脂筏结合的分子机制是细胞生物学和医学中的核心问题。在靶向脂筏的不相关细胞和微生物蛋白中已鉴定出一种结构保守基序（“鞘脂结合结构域”）。我提出，围绕鞘脂结合结构域形成的鞘脂壳不仅能将蛋白质从质膜的液相无序相中提取出来，并确保其被递送至脂筏，还会影响其构象。鞘脂在壳和脂筏中的伴侣活性可能在感染性疾病和构象性疾病（人类免疫缺陷病毒1型、朊病毒、阿尔茨海默病）中发挥重要作用。
