Füllekrug Joachim, Simons Kai
Max-Planck-Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Ann N Y Acad Sci. 2004 Apr;1014:164-9. doi: 10.1196/annals.1294.017.
Lipid rafts are dynamic assemblies floating freely in the surrounding membranes of living cells. This membrane heterogeneity provides a useful concept for understanding processes as diverse as cell polarity, signal transduction, and membrane sorting. Individual rafts are small entities containing thousands of lipids but only a few proteins. Regulation of raft association and size is an elementary feature of interactions at the molecular level. By clustering small rafts into a bigger platform, proteins are brought together for modification. Oligomerization might transform a monomeric weakly raft-associated protein into an assembly with higher raft affinity. Lectins are multivalent glycoprotein-binding proteins and are likely to be key players in mediating the clustering of rafts in vivo. Glycosylation-dependent surface delivery in a polarized fashion is a feature conserved across evolution, and we expect lectins to be at the heart of the molecular machinery responsible for lipid raft delivery to the cell surface. Currently, we are evaluating candidate proteins by affinity chromatography, proteomics, and RNA interference.
脂筏是动态组装体,在活细胞的周围膜中自由漂浮。这种膜的异质性为理解细胞极性、信号转导和膜分选等多种过程提供了一个有用的概念。单个脂筏是包含数千种脂质但只有少数蛋白质的小实体。脂筏缔合和大小的调节是分子水平相互作用的基本特征。通过将小脂筏聚集成更大的平台,蛋白质聚集在一起进行修饰。寡聚化可能会将单体的弱脂筏相关蛋白转化为具有更高脂筏亲和力的组装体。凝集素是多价糖蛋白结合蛋白,可能是体内介导脂筏聚集的关键参与者。以极化方式进行的糖基化依赖性表面递送是进化过程中保守的特征,我们预计凝集素是负责将脂筏递送至细胞表面的分子机制的核心。目前,我们正在通过亲和色谱、蛋白质组学和RNA干扰评估候选蛋白。