The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity
The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity
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DOI：
10.1074/jbc.m010647200
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发表时间：
2001-04-06
影响因子：
4.8
通讯作者：
Volkmer, H
中科院分区：
文献类型：
--
作者：
Koroll, M;Rathjen, FG;Volkmer, H
神经束蛋白属于细胞粘附分子免疫球蛋白超家族的L1亚群，与轴突生长和束状形成有关。我们使用酵母双杂交筛选来鉴定细胞内与神经束蛋白相互作用的蛋白，因此可能将其与运输，空间靶向或信号通路联系起来。在这里，我们证明大鼠syntenin-1，先前发表为syntenin， mda-9或TACIP18，是一种神经束蛋白结合蛋白，表现出广泛的组织表达模式，在大脑中相对最多。我们发现Syntenin-1不与L1亚群的其他脊椎动物成员（如L1本身或NrCAM）相互作用。我们通过配体覆盖试验、表面等离子体共振分析和两种蛋白在异源细胞中的共定位证实了神经束蛋白- Syntenin-1相互作用的特异性。神经束蛋白的COOH末端被定位为与syntenin-1的第二个PDZ结构域相互作用。此外，我们分离出可能以两种亚型表达的syntenin-2，尽管它们与syntenin-1的序列高度相似，syntenin-2 α与神经rexin I相互作用，syntenin-2 β不与神经束蛋白或其他几种作为syntenin-1结合伙伴的跨膜蛋白结合。最后，我们报道syntenin-1和-2都形成同型二聚体，并且可以相互作用。
Neurofascin belongs to the L1 subgroup of the immunoglobulin superfamily of cell adhesion molecules and is implicated in axonal growth and fasciculation, We used yeast two-hybrid screening to identify proteins that interact with neurofascin intracellularly and therefore might link it to trafficking, spatial targeting, or signaling pathways, Here, we demonstrate that rat syntenin-1, previously published as syntenin, mda-9, or TACIP18 in human, is a neurofascin-binding protein that exhibits a wide-spread tissue expression pattern with a relative maximum in brain. Syntenin-1 was found not to interact with other vertebrate members of the L1 subgroup such as L1 itself or NrCAM, We confirmed the specificity of the neurofascin-syntenin-1 interaction by ligand-overlay assay, surface plasmon resonance analysis, and colocalization of both proteins in heterologous cells. The COOH terminus of neurofascin was mapped to interact with the second PDZ domain of syntenin-1. Furthermore, we isolated syntenin-2 that may be expressed in two isoforms, Despite their high sequence similarity to syntenin-1, syntenin-2 alpha, which interacts with neurexin I, and syntenin-2 beta do not bind to neurofascin or several other transmembrane proteins that are binding partners of syntenin-1, Finally, we report that syntenin-1 and -2 both form homodimers and can interact with each other.