THE CYTOPLASMIC DOMAIN OF THE DROSOPHILA CELL-ADHESION MOLECULE NEUROGLIAN IS NOT ESSENTIAL FOR ITS HOMOPHILIC ADHESIVE PROPERTIES IN S2 CELLS
THE CYTOPLASMIC DOMAIN OF THE DROSOPHILA CELL-ADHESION MOLECULE NEUROGLIAN IS NOT ESSENTIAL FOR ITS HOMOPHILIC ADHESIVE PROPERTIES IN S2 CELLS
复制标题
DOI：
10.1074/jbc.270.32.18809
复制
发表时间：
1995-08-11
影响因子：
4.8
通讯作者：
BIEBER, AJ
中科院分区：
文献类型：
--
作者：
HORTSCH, M;WANG, YME;BIEBER, AJ
果蝇神经胶质细胞是一种跨膜糖蛋白，其与脊椎动物细胞粘附分子的L1基因家族具有很强的结构和序列同源性（比伯，AJ.，斯诺，下午，Hortsch，M.，帕特尔，北H、雅各布斯，J.R.，Traquina，Z. R.，Schilling，J.，和Goodman，C. S.（1989）Cell 59，447-460）。由差异剪接过程产生的两种不同的神经胶质蛋白形式由胚胎和幼虫细胞以组织特异性方式表达（Hortsch，M.，比伯，A. J.，帕特尔，北H、和Goodman，C. S.等（1990）Neuron 4，697-709）。这两种神经胶质多肽仅在其胞质结构域中不同。这两种神经胶质细胞，当转染到果蝇S2细胞中表达时，诱导转化细胞的钙非依赖性，嗜同性聚集。第三种人工神经胶质蛋白形式通过用果蝇fasciclin I蛋白的糖基磷脂酰肌醇附着信号取代神经胶质跨膜区段和胞质结构域来构建。该cDNA构建体产生糖基磷脂酰肌醇锚定形式的神经胶质细胞，其在S2细胞中表达时保留诱导嗜同性细胞聚集的能力，并且能够与两种天然存在的神经胶质多肽相互作用。这些结果表明，神经胶质细胞介导的钙依赖性，嗜同性细胞粘附活性，既不是细胞质神经胶质结构域，也不是与细胞骨架元素的直接相互作用是必不可少的这个属性。
Drosophila neuroglian is a transmembrane glycoprotein that has strong structural and sequence homology to the vertebrate L1 gene family of cell adhesion molecules (Bieber, A J., Snow, P. M., Hortsch, M., Patel, N. H., Jacobs, J. R., Traquina, Z. R., Schilling, J., and Goodman, C. S. (1989) Cell 59, 447-460). Two different neuroglian protein forms that are generated by a differential splicing process are expressed in a tissue-specific fashion by embryonic and larval cells (Hortsch, M., Bieber, A. J., Patel, N. H., and Goodman, C. S. (1990) Neuron 4, 697-709). The two neuroglian polypeptides differ only in their cytoplasmic domains. Both of these neuroglian species, when transfected into and expressed in Drosophila S2 cells, induce the calcium-independent, homophilic aggregation of transformed cells. A third artificial neuroglian protein form was constructed by substituting the neuroglian transmembrane segment and cytoplasmic domains with the glycosyl phosphatidylinositol attachment signal of the Drosophila fasciclin I protein. This cDNA construct generates a glycosyl phosphatidylinositol-anchored form of neuroglian, which retains the ability to induce homophilic cell aggregation when expressed in S2 cells, and was able to interact with both of the two naturally occurring neuroglian polypeptides. These results demonstrate that neuroglian mediates a calcium-independent, homophilic cell adhesion activity and that neither cytoplasmic neuroglian domains nor a direct interaction with cytoskeletal elements is essential for this property.