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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Co-purification and localization of Munc18-1 (p67) and Cdk5 with neuronal cytoskeletal proteins.
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Co-purification and localization of Munc18-1 (p67) and Cdk5 with neuronal cytoskeletal proteins.

机译：Munc18-1（p67）和Cdk5与神经元细胞骨架蛋白的共纯化和定位。

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摘要

Munc18-1 (p67, nSec1, rbSec1), a neuron-specific 67kDa protein was independently identified as a syntaxin-binding protein, and as a component that co-purifies with, and regulates the kinase activity of cyclin dependent kinase (Cdk5). Gene knockout studies have demonstrated a role for Munc18-1 in synaptic vesicle docking and neurotransmitter release. Mice lacking Munc18-1 gene were synaptically silent, but the gene deletion did not prevent normal brain assembly, including the formation of layered structures, fiber pathways and morphologically defined synapses. Previous study has shown that Munc18-1 facilitates Cdk5 mediated phosphorylation of KSPXK domains of the neuronal cytoskeletal elements, suggesting that Munc18-1 may function in the regulation of cytoskeletal dynamics. Present study demonstrates the co-purification and co-localization of Munc18 with cytoskeletal elements and forms first step towards understanding the role for Munc18-1 in cytoskeletal dynamics. Conversely, the cytoskeletal proteinsand Cdk5 co-purifies with Munc18-1 in a Munc18-1 immuno-affinity chromatography, suggesting a strong protein-protein interaction. Findings from immunofluorescence studies in PC12 cells have shown co-localization of Munc18-1 and Cdk5 with neurofilaments and microtubules. Further, immunohistochemical and immuno-electron microscopic studies of rat olfactory bulb also demonstrated co-localization of Munc18-1 and Cdk5 with cytoskeletal elements. Thus, the biochemical evidence of strong interaction between Munc18-1 with cytoskeletal proteins and morphological evidence of their (Munc18 and cytoskeletal elements) identical sub-cellular localization is suggestive of the possible role for Munc18-1 in cytoskeletal dynamics.
机译：Munc18-1（p67，nSec1，rbSec1）是一种神经元特异性67kDa蛋白，被独立鉴定为语法素结合蛋白，并且是与细胞周期蛋白依赖性激酶（Cdk5）共纯化并调节其激酶活性的组分。基因敲除研究已证明Munc18-1在突触小泡对接和神经递质释放中的作用。缺少Munc18-1基因的小鼠突触沉默，但基因缺失并不能阻止正常的大脑组装，包括分层结构，纤维途径和形态学确定的突触的形成。先前的研究表明Munc18-1促进Cdk5介导的神经元细胞骨架KSPXK域的磷酸化，提示Munc18-1可能在细胞骨架动力学的调节中起作用。本研究证明了Munc18与细胞骨架成分的共纯化和共定位，并且是迈向了解Munc18-1在细胞骨架动力学中作用的第一步。相反，在Munc18-1免疫亲和色谱中，细胞骨架蛋白和Cdk5与Munc18-1共纯化，表明强烈的蛋白-蛋白相互作用。在PC12细胞中进行的免疫荧光研究发现，Munc18-1和Cdk5与神经丝和微管共定位。此外，大鼠嗅球的免疫组织化学和免疫电子显微镜研究也证明了Munc18-1和Cdk5与细胞骨架成分共定位。因此，Munc18-1与细胞骨架蛋白之间强烈相互作用的生化证据以及它们（Munc18和细胞骨架元素）相同的亚细胞定位的形态学证据表明，Munc18-1在细胞骨架动力学中的可能作用。

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