Functionally different GPI proteins are organized in different domains on the neuronal surface
Functionally different GPI proteins are organized in different domains on the neuronal surface
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DOI：
10.1093/emboj/18.24.6917
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发表时间：
1999-12-15
期刊：
影响因子：
11.4
通讯作者：
Morris, R
中科院分区：
文献类型：
--
作者：
Madore, N;Smith, KL;Morris, R
我们已经调查了组织，在质膜和洗涤剂不溶性膜囊泡，两个神经元糖基磷脂酰肌醇锚定（GPI）蛋白：Thy-1，负调节跨膜信号转导;和朊病毒蛋白，其快速内吞作用和Cu 2+结合表明，它的功能在金属离子摄取。朊病毒蛋白以高密度分布在神经元表面，主要位于细胞体，相对可溶于去污剂。Thy-1虽然在神经元上表达丰富得多，但在对去污剂溶解具有高度抗性的结构域中，在神经突的大部分表面上以较低的密度出现，在细胞体上以较低的丰度出现。去污剂不溶性膜囊泡以与神经元表面上的密度相似的密度含有Thy-1。含有每种蛋白质的囊泡可以通过免疫亲和分离分离;凝集素结合表明它们富含不同的糖蛋白。我们的研究结果表明，功能不同的GPI蛋白质所占据的结构域的多样性。
We have investigated the organization, on the plasma membrane and in detergent-insoluble membrane vesicles, of two neuronal glycosylphosphatidylinositol-anchored (GPI) proteins: Thy-1, a negative regulator of transmembrane signalling; and prion protein, whose rapid endocytosis and Cu2+ binding suggest that it functions in metal ion uptake. Prion protein occurred on the neuronal surface at high density in domains, located primarily at the cell body, which were relatively soluble in detergent. Thy-1, although much more abundantly expressed on neurons, occurred at lower density over much of the surface of neurites land in lower abundance at the cell body) in domains that were highly resistant to detergent solubilization, Detergent-insoluble membrane vesicles contained Thy-1 at a density similar to that on the neuronal surface. Vesicles containing each protein could be separated by immunoaffinity isolation; lectin binding showed that they were enriched in different glycoproteins. Our results demonstrate a structural diversity of the domains occupied by functionally different GPI proteins.