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Spatial signal repression as an additional role of Sprouty2 protein variants

机译：空间信号压制作为Sprouty2蛋白质变异的额外作用

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Sprouty2 (Spry2) is a prominent member of a protein family with crucial functions in the modulation of signal transduction. One of its main actions is the repression of mitogen-activated protein kinase (MAPK) pathway in response to growth factor-induced signalling. A common single nucleotide polymorphism within the Spry2 gene creates two protein variants where a proline adjacent to the serine rich domain is converted to an additional serine. Both protein variants perform similar functions although their efficiency in fulfilling these tasks varies. In this report, we used biochemical fractionation methods as well as confocal microscopy to analyse quantitative and qualitative differences in the distribution of Spry2 variants. We found that Spry2 proteins localize not solely to the plasma membrane, but also to other membrane engulfed compartments like for example the Golgi apparatus. In these less dense organelles, predominantly slower migrating forms reside indicating that post translational modification contributes to the distribution profile of Spry2. However there is no significant difference in the distribution of the two variants. Additionally, we found that Spry2 could be found exclusively in membrane fractions irrespective of the mitogen availability and the phosphorylation status. Considering the interference of extracellular signal-regulated kinase (ERK) activation in the cytoplasm, both Spry2 variants inhibited the levels of phosphorylated ERK (pERK) significantly to a similar extent. In contrast, the induction profiles of pERK levels were completely different in the nuclei. Again, both Spry2 variants diminished the levels of pERK. While the proline variant lowered the activation throughout the observation period, the serine variant failed to interfere with immediate accumulation of nuclear pERK levels, but the signal duration was shortened. Since the extent of the pERK inhibition in the nuclei was drastically more pronounced than in the cytoplasm, we conclu
机译：Sprouty2（Spry2）是蛋白质家族的突出成分，具有在信号转导的调节中具有重要功能。其主要作用之一是响应于生长因子诱导的信号传导抑制丝裂原激活的蛋白激酶（MAPK）途径。 Spry2基因内的常见单核苷酸多态性产生了两种蛋白质变体，其中与富丝氨酸域的脯氨酸转化为另外的丝氨酸。蛋白质变体都执行类似的功能，尽管它们实现这些任务的效率变化。在本报告中，我们使用生化分馏方法以及共聚焦显微镜，分析了Spry2变体分布的定量和定性差异。我们发现Spry2蛋白不仅本地化到质膜，而且对其他膜吞噬隔室也是如例如例如GOLGI装置的膜。在这些较少的致密细胞器中，主要迁移形式升级，表明翻译后修改有助于SPRy2的分布曲线。然而，两种变体的分布没有显着差异。另外，我们发现，无论有丝分裂原性和磷酸化状态如何，都可以在膜级分中仅发现SPRy2。考虑到细胞质中细胞外信号调节激酶（ERK）活化的干扰，两种SPRY2变体抑制了磷酸化ERK（PERK）的水平在类似的程度上。相比之下，核水平的诱导谱在核中完全不同。同样，两个SPry2变体都减少了Perk的水平。虽然脯氨酸变体在整个观察期间降低了激活，但丝氨酸变化未能干扰核开核水平的立即积累，但信号持续时间缩短。由于核在细胞核中的Perk抑制程度比在细胞质中众所周大，因此我们得到了总结

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