Cullin-RING ubiquitin ligases in salicylic acid-mediated plant immune signaling.

Cullin-RING ubiquitin ligases in salicylic acid-mediated plant immune signaling.
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DOI:
10.3389/fpls.2015.00154
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发表时间:
2015
影响因子:
5.6
通讯作者:
Spoel SH
Spoel SH
中科院分区:
生物学2区
文献类型:
--
作者:
Furniss JJ;Spoel SH

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植物对生物营养病原体的免疫应答是由信号激素水杨酸(SA)调节的。SA通过调节多种细胞过程,包括程序性细胞死亡(PCD)来分离和杀死入侵的病原体,以及系统获得性抗性(SAR)的发展,从而在整个植物中提供持久的广谱抗性,从而建立免疫力。这些过程的核心是通过泛素化,即小泛素蛋白的共价添加,对sa调节的信号蛋白进行翻译后修饰。新出现的证据表明,sa诱导的蛋白质泛素化在很大程度上是由Cullin-RING连接酶(CRLs)精心策划的,它通过可互换的接头招募特定的底物进行泛素化。在赖氨酸48处连接的泛素链的连接导致底物被26S蛋白酶体降解。在这里,我们讨论了含有核苷酸结合/富含亮氨酸重复结构域的免疫受体和sa诱导的转录调节因子如何介导的降解分别对功能性PCD和SAR反应至关重要。通过将这些最近的发现与其他真核模式物种的知识结合起来,我们强调了在调节sa介导的免疫反应活性中,过程泛素化的潜在替代作用。
Plant immune responses against biotrophic pathogens are regulated by the signaling hormone salicylic acid (SA). SA establishes immunity by regulating a variety of cellular processes, including programmed cell death (PCD) to isolate and kill invading pathogens, and development of systemic acquired resistance (SAR) which provides long-lasting, broad-spectrum resistance throughout the plant. Central to these processes is post-translational modification of SA-regulated signaling proteins by ubiquitination, i.e., the covalent addition of small ubiquitin proteins. Emerging evidence indicates SA-induced protein ubiquitination is largely orchestrated by Cullin-RING ligases (CRLs), which recruit specific substrates for ubiquitination using interchangeable adaptors. Ligation of ubiquitin chains interlinked at lysine 48 leads to substrate degradation by the 26S proteasome. Here we discuss how CRL-mediated degradation of both nucleotide-binding/leucine-rich repeat domain containing immune receptors and SA-induced transcription regulators are critical for functional PCD and SAR responses, respectively. By placing these recent findings in context of knowledge gained in other eukaryotic model species, we highlight potential alternative roles for processive ubiquitination in regulating the activity of SA-mediated immune responses.
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