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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Mapping FLS2 function to structure: LRRs, kinase and its working bits
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Mapping FLS2 function to structure: LRRs, kinase and its working bits

机译:将FLS2功能映射到结构:LRR,激酶及其工作位

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摘要

The plasma membrane-localised FLAGELLIN SENSING 2 (FLS2) receptor is an important component of plant immunity against potentially pathogenic bacteria, acting to recognise the conserved flg22 peptide of flagellin. FLS2 shares the common structure of transmembrane receptor kinases with a receptor-like ectodomain composed of leucine-rich repeats (LRR) and an active intracellular kinase domain. Upon ligand binding, FLS2 dimerises with the regulatory LRR-receptor kinase BRI1-associated kinase 1, which in turn triggers downstream signalling cascades. Although lacking crystal structure data, recent advances have been made in our understanding of flg22 recognition based on structural and functional analyses of FLS2. These studies have revealed critical regions/residues of FLS2 and post-translational modifications that regulate the abundance and activity of this receptor. In this review, we present the current knowledge on the structural mechanism of the FLS2-flg22 interaction and subsequent receptor-mediated signalling.
机译:质膜定位的FLAGELLIN SENSING 2(FLS2)受体是植物针对潜在病原细菌的免疫力的重要组成部分,其作用是识别鞭毛蛋白的保守flg22肽。 FLS2具有跨膜受体激酶的共同结构,该结构具有由富含亮氨酸的重复序列(LRR)和活性细胞内激酶域组成的受体样胞外域。配体结合后,FLS2与调节性LRR受体激酶BRI1相关的激酶1二聚,进而触发下游信号传导级联。尽管缺乏晶体结构数据,但基于FLS2的结构和功能分析,我们对flg22识别的理解取得了最新进展。这些研究揭示了FLS2的关键区域/残基和翻译后修饰,这些修饰调节了该受体的丰度和活性。在这篇综述中,我们介绍了FLS2-flg22相互作用和随后的受体介导的信号传导的结构机理的当前知识。

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