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首页> 外文期刊>The European Journal of Neuroscience >CNTNAP2 is targeted to endosomes by the polarity protein PAR3
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CNTNAP2 is targeted to endosomes by the polarity protein PAR3

机译：CNTNAP2由极性蛋白PAR3靶向内体

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A decade of genetic studies has established contactin-associated protein-like 2 (CNTNAP2) as a prominent susceptibility gene associated with multiple neurodevelopmental disorders. The development and characterization of Cntnap2 knockout models in multiple species have bolstered this claim by establishing clear connections with certain endophenotypes. Despite these remarkable in vivo findings, CNTNAP2's molecular functions are relatively unexplored, highlighting the need to identify novel protein partners. Here, we characterized an interaction between CNTNAP2 and partitioning-defective 3 (PAR3)-a polarity molecule isolated in a yeast two-hybrid screen with CNTNAP2's C-terminus. We provide evidence that the two proteins interact via PDZ domain-mediated binding, that CNTNAP2(+)/PAR3(+) complexes are largely associated with clathrin-coated endocytic vesicles in heterologous cells and that PAR3 causes an enlargement of CNTNAP2 puncta size. Live imaging and fluorescence recovery after photobleaching (FRAP) reveals that PAR3 limits the mobility of CNTNAP2. Finally, overexpression of PAR3 but not a PAR3 mutant lacking all PDZ domains (PAR3 increment PDZall) can cluster endogenous CNTNAP2 in primary neurons. Collectively, we conclude that PAR3 regulates CNTNAP2 spatial localization.
机译：遗传研究的十年已经建立了与多种神经发育障碍相关的突出易感基因的接触蛋白相关的蛋白质2（CNTNAP2）。多种物种中CNTNAP2敲除模型的开发和表征通过建立了与某些内卵素的清晰连接而引起了这种索赔。尽管体内调查结果表明，CNTNAP2的分子功能相对未开发，突出了识别新型蛋白质合作伙伴的需要。这里，我们表征了CNTNAP2和分配缺陷3（PAR3）-A极性分子与CNTNAP2的C-末端中分离的分离的分离的缺陷3（PAR3）极性分子之间的相互作用。我们提供了通过PDZ结构域介导的结合的两种蛋白质相互作用，即CNTNAP2（+）/ pAR3（+）络合物在异源细胞中的克拉螯盐涂覆的内吞囊泡很大程度上与CNTNAP2斑隙尺寸的放大引起。摄影博丁化（FRAP）后的实时成像和荧光恢复表明PAR3限制了CNTNAP2的迁移率。最后，PAR3的过度表达但不是缺乏所有PDZ结构域的PAR3突变体（PAR3增量PDZALL）可以在原发性神经元中纳入内源性CNTNAP2。总的来说，我们得出结论，PAR3规范了CNTNAP2空间定位。

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