PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands
PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands
复制标题
DOI：
10.1016/s0896-6273(00)80663-7
复制
发表时间：
1998-12-01
期刊：
影响因子：
16.2
通讯作者：
Yancopoulos, GD
中科院分区：
文献类型：
--
作者：
Torres, R;Firestein, BL;Yancopoulos, GD
将细胞表面受体定位于特定的亚细胞位置对于它们的正常功能可能是至关重要的，如在神经元突触中最显著地证明的。PDZ蛋白显然在这种蛋白定位中起关键作用。受体酪氨酸激酶以前没有显示与脊椎动物中的PDZ蛋白相互作用。我们报告说，Eph受体和它们的膜连接配体都含有PDZ识别基序，并可以结合和聚集的PDZ蛋白。此外，我们发现Eph受体和配体与PDZ蛋白共定位于突触。因此，PDZ蛋白可能在定位脊椎动物受体酪氨酸激酶和/或其配体中发挥关键作用，并且可能对Eph在指导或模式化或突触中的功能特别重要。
Localizing cell surface receptors to specific subcellular positions can be critical for their proper functioning, as most notably demonstrated at neuronal synapses. PDZ proteins apparently play critical roles in such protein localizations. Receptor tyrosine kinases have not been previously shown to interact with PDZ proteins in vertebrates. We report that Eph receptors and their membrane-linked ligands all contain PDZ recognition motifs and can bind and be clustered by PDZ proteins. In addition, we find that Eph receptors and ligands colocalize with PDZ proteins at synapses. Thus, PDZ proteins may play critical roles in localizing vertebrate receptor tyrosine kinases and/or their ligands and may be particularly important for Eph function in guidance or patterning or at the synapse.