Uchida Yoko, Gomi Fujiya
Research Team for Aging Neuroscience, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.
Neuroreport. 2015 Dec 16;26(18):1140-4. doi: 10.1097/WNR.0000000000000486.
β-Amyloid is generated by the sequential cleavage of amyloid precursor protein. Calsyntenin-1 and kinesin light chain-1 splice variant E (KLC1-E) have been proposed to regulate β-amyloid production from amyloid precursor protein. Vesicles containing calsyntenin-1 are transported from the Golgi apparatus to axons by interaction between calsyntenin-1 and KLC1 in their C-terminal regions. However, it is unclear whether KLC1 isoform E influences the interaction between KLC1 and calsyntenin-1, resulting in the impaired axonal transport of calsyntenin-1 vesicles. Here, we show that KLC1-E does not interact with calsyntenin-1 using a pull-down assay, coimmunoprecipitation, and immunocytochemistry. These findings suggest that KLC1-E enrichment may impair the axonal transport of calsyntenin-1 vesicles.
β-淀粉样蛋白由淀粉样前体蛋白的顺序切割产生。钙联蛋白-1和驱动蛋白轻链-1剪接变体E（KLC1-E）被认为可调节淀粉样前体蛋白产生β-淀粉样蛋白的过程。含有钙联蛋白-1的囊泡通过其C末端区域的钙联蛋白-1与KLC1之间的相互作用从高尔基体运输到轴突。然而，尚不清楚KLC1同工型E是否会影响KLC1与钙联蛋白-1之间的相互作用，从而导致钙联蛋白-1囊泡的轴突运输受损。在这里，我们通过下拉分析、免疫共沉淀和免疫细胞化学表明KLC1-E不与钙联蛋白-1相互作用。这些发现表明KLC1-E的富集可能会损害钙联蛋白-1囊泡的轴突运输。
