Hortsch M, Goodman C S
Howard Hughes Medical Institute, University of California, Berkeley 94720.
J Biol Chem. 1990 Sep 5;265(25):15104-9.
Fasciclin I is a homophilic neural cell adhesion molecule which is regionally expressed on a subset of fasciculating axons in both the grasshopper and Drosophila embryo, suggesting a role in axonal recognition. It is also dynamically expressed on a variety of other embryonic tissues. Biochemical analysis of the fasciclin I glycoprotein from Drosophila embryonic membranes and Schneider 1 cells indicates that it is tightly associated with the lipid bilayer by a phosphatidylinositol lipid moiety. In Drosophila embryos a large fraction of fasciclin I protein has lost its membrane anchor. The ratio of this soluble form to the phosphatidylinositol-linked form changes during embryogenesis. We speculate that removal of the phosphatidylinositol lipid from the fasciclin I protein could be a mechanism to regulate its adhesive function.
成束蛋白I是一种同源性神经细胞黏附分子，在蚱蜢和果蝇胚胎中，它在成束轴突的一个亚群上呈区域表达，这表明它在轴突识别中发挥作用。它也在多种其他胚胎组织上动态表达。对来自果蝇胚胎膜和施奈德1细胞的成束蛋白I糖蛋白进行生化分析表明，它通过磷脂酰肌醇脂质部分与脂质双层紧密相连。在果蝇胚胎中，大部分成束蛋白I蛋白已失去其膜锚定。这种可溶性形式与磷脂酰肌醇连接形式的比例在胚胎发育过程中发生变化。我们推测，从成束蛋白I蛋白上去除磷脂酰肌醇脂质可能是一种调节其黏附功能的机制。
