Eukaryotic signal transduction via histidine-aspartate phosphorelay.
Eukaryotic signal transduction via histidine-aspartate phosphorelay.
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发表时间：
2000-09
影响因子：
4
通讯作者：
P. Thomason;R. Kay
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作者：
P. Thomason;R. Kay
跨膜信号转导是所有真核和原核细胞共有的特征。我们现在了解到，真核生物和原核生物使用的信号机制的子集不仅在原则上相似，而且实际上使用同源蛋白质。这些是组氨酸-天冬氨酸磷酸传递，真细菌起源的信号系统，现在已知广泛存在于动物界以外的真核生物中。基因组计划揭示，His-Asp磷酸化继电器作为多基因家族存在于低等真核生物和植物中。一个主要的挑战是了解这些“新的”信号转导系统如何与真核细胞中存在的更熟悉的信号传导机制形成集成网络。磷酸化继电器已经被表征为调节MAP激酶级联和cAMP/PKA途径。动物中可能不存在His-Asp磷酸化继电器，这引起了人们对它们作为抗微生物治疗（包括抗真菌药）靶点的潜力的兴趣。最近的研究结果表明，这种方法有希望。
Transmembrane signal transduction is a feature common to all eukaryotic and prokaryotic cells. We now understand that a subset of the signalling mechanisms used by eukaryotes and prokaryotes are not just similar in principle, but actually use homologous proteins. These are the histidine-aspartate phosphorelays, signalling systems of eubacterial origin, now known to be widespread in eukaryotes outside the animal kingdom. Genome projects are revealing that His-Asp phosphorelays are present as multigene families in lower eukaryotes and in plants. A major challenge is to understand how these 'novel' signal transduction systems form integrated networks with the more familiar signalling mechanisms also present in eukaryotic cells. Already, phosphorelays have been characterised that regulate MAP kinase cascades and the cAMP/PKA pathway. The probable absence of His-Asp phosphorelays from animals has generated interest in their potential as targets for anti-microbial therapy, including antifungals. Recent findings suggest that this approach holds promise.