CHARACTERIZATION AND GENE CLONING OF NEUROTACTIN, A DROSOPHILA TRANSMEMBRANE PROTEIN RELATED TO CHOLINESTERASES
CHARACTERIZATION AND GENE CLONING OF NEUROTACTIN, A DROSOPHILA TRANSMEMBRANE PROTEIN RELATED TO CHOLINESTERASES
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DOI：
10.1002/j.1460-2075.1990.tb07570.x
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发表时间：
1990-11-01
期刊：
影响因子：
11.4
通讯作者：
JIMENEZ, F
中科院分区：
文献类型：
--
作者：
DELAESCALERA, S;BOCKAMP, EO;JIMENEZ, F
单抗已用于表征神经触动蛋白，一种新的果蝇蛋白，其在细胞黏附中的作用被推测。表位定位和氨基酸序列表明，Neurotactin是一种跨膜蛋白。与其他细胞黏附分子类似，神经触动蛋白在表达神经触动蛋白的细胞相互接触的细胞膜部分积聚。该蛋白仅在细胞增殖和分化过程中检测到，主要存在于神经组织中，也存在于中胚层和成像盘中。Neurotactin有一个大的细胞质结构域，富含带电残基，而胞外结构域类似于胆碱酯酶，缺乏酯酶活性所需的活性部位丝氨酸。胞外结构域还包含三个拷贝的亮氨酸-精氨酸-谷氨酸三肽，这个基序构成了脊椎动物S-层粘连蛋白粘连位点的主要序列。
Monoclonal antibodies have served to characterize neurotactin, a novel Drosophila protein for which a role in cell adhesion is postulated. Neurotactin is a transmembrane protein, as indicated by epitope mapping and amino acid sequence. Similarly to other cell adhesion molecules, neurotactin accumulates in parts of the membrane where neurotactin‐expressing cells contact each other. The protein is only detected during cell proliferation and differentiation, and it is found mainly in neural tissue and also in mesoderm and imaginal discs. Neurotactin has a large cytoplasmic domain rich in charged residues and an extracellular domain similar to cholinesterase that lacks the active site serine required for esterase activity. The extracellular domain also contains three copies of the tripeptide leucine‐arginine‐glutamate, a motif that forms the primary sequence of the adhesive site of vertebrate s‐laminin.