Alternative complex formation of the Ca2+-regulated protein kinase CIPK1 controls abscisic acid-dependent and independent stress responses in Arabidopsis

Alternative complex formation of the Ca2+-regulated protein kinase CIPK1 controls abscisic acid-dependent and independent stress responses in Arabidopsis
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DOI:
10.1111/j.1365-313x.2006.02921.x
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发表时间:
2006-12-01
期刊:
影响因子:
7.2
通讯作者:
Kudla, Joerg
Kudla, Joerg
中科院分区:
生物学1区
文献类型:
--
作者:
D'Angelo, Cecilia;Weinl, Stefan;Kudla, Joerg

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细胞内钙离子释放属于细胞应激感知的最早事件。整合来自不同环境信号并将其转化为优化反应的分子机制在很大程度上是未知的。我们在这里报道了CIPK1的功能特征,CIPK1是一种与钙传感器CBL1和CBL9强烈相互作用的蛋白激酶。表达模式的比较表明,这三种蛋白在同一组织中执行其功能。CIPK1与CBL1和CBL9的物理相互作用将激酶靶向到质膜上。我们发现,与CBL9功能的丧失类似,CBL1或CIPK1的突变会使植物对渗透胁迫过敏。值得注意的是,与cbl1突变体和cbl9突变体相比,CIPK1功能的丧失会损害脱落酸(ABA)的响应性。因此,我们认为,通过与CBL1或CBL9交替形成复合物,CIPK1激酶代表了aba依赖性和aba非依赖性应激反应的趋同点。基于我们的遗传、生理和蛋白质-蛋白质相互作用数据,我们提出了钙调节信号网络中信息处理的一般模型。
Intracellular release of calcium ions belongs to the earliest events in cellular stress perception. The molecular mechanisms integrating signals from different environmental cues and translating them into an optimized response are largely unknown. We report here the functional characterization of CIPK1, a protein kinase interacting strongly with the calcium sensors CBL1 and CBL9. Comparison of the expression patterns indicates that the three proteins execute their functions in the same tissues. Physical interaction of CIPK1 with CBL1 and CBL9 targets the kinase to the plasma membrane. We show that, similarly to loss of CBL9 function, mutation of either CBL1 or CIPK1 renders plants hypersensitive to osmotic stress. Remarkably, in contrast to the cbl1 mutant and similarly to the cbl9 mutant, loss of CIPK1 function impairs abscisic acid (ABA) responsiveness. We therefore suggest that, by alternative complex formation with either CBL1 or CBL9, the kinase CIPK1 represents a convergence point for ABA-dependent and ABA-independent stress responses. Based on our genetic, physiological and protein-protein interaction data, we propose a general model for information processing in calcium-regulated signalling networks.