Protein Phosphorylation Dynamics Under Carbon/Nitrogen-Nutrient Stress and Identification of a Cell Death-Related Receptor-Like Kinase in Arabidopsis
Protein Phosphorylation Dynamics Under Carbon/Nitrogen-Nutrient Stress and Identification of a Cell Death-Related Receptor-Like Kinase in Arabidopsis
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DOI：
10.3389/fpls.2020.00377
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发表时间：
2020-04
影响因子：
5.6
通讯作者：
Xingwen Li;Miho Sanagi;Yu Lu;Y. Nomura;S. Stolze;Shigetaka Yasuda;Y. Saijo;W. Schulze;R. Feil;M. Stitt;J. Lunn;Hirofumi Nakagami;Takeo Sato;J. Yamaguchi
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文献类型：
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作者：
Xingwen Li;Miho Sanagi;Yu Lu;Y. Nomura;S. Stolze;Shigetaka Yasuda;Y. Saijo;W. Schulze;R. Feil;M. Stitt;J. Lunn;Hirofumi Nakagami;Takeo Sato;J. Yamaguchi
养分的可利用性，特别是糖[碳（C）]和氮（N）的可利用性，对于调节植物的代谢和发育是重要的。除了独立利用C和N营养外，植物还感知并响应它们可利用的C和N营养（C/N营养）的平衡。高C/低N营养胁迫已被证明可以阻止拟南芥萌发后早期的生长，同时促进衰老的进程。虽然已经鉴定了C/N-营养响应的几个信号组分，但植物C/N-营养响应的分子基础仍然不清楚。该蛋白质组分析评估了响应高C/低N营养胁迫的磷酸化动力学。磷蛋白质组学研究表明，在C/N营养胁迫条件下，质膜H+-ATPase、碳氮代谢酶以及蛋白激酶、转录因子等信号蛋白的磷酸化状态发生了全面的变化。进一步的分析表明，SNF 1相关蛋白激酶1（SnRK 1）通过C/N调节激酶的转录调节参与主要的C/N营养信号介导。我们还鉴定了一个富含亮氨酸的重复序列受体样激酶，命名为LMK 1，它具有诱导植物叶片细胞死亡的活性。这些结果提供了重要的洞察C/N-营养信号通路连接营养胁迫的各种细胞和生理过程中的植物。
Nutrient availability, in particular the availability of sugar [carbon (C)] and nitrogen (N), is important for the regulation of plant metabolism and development. In addition to independent utilization of C and N nutrients, plants sense and respond to the balance of C and N nutrients (C/N-nutrient) available to them. High C/low N-nutrient stress has been shown to arrest early post-germinative growth while promoting progression to senescence in Arabidopsis. Although several signaling components of the C/N-nutrient response have been identified, the inclusive molecular basis of plant C/N-nutrient response remains unclear. This proteome analysis evaluated phosphorylation dynamics in response to high C/low N-nutrient stress. Phosphoproteomics under conditions of C/N-nutrient stress showed a global change in the phosphorylation status of proteins, including plasma membrane H+-ATPase, carbon and nitrogen metabolic enzymes and signaling proteins such as protein kinases and transcription factors. Further analyses suggested that SNF1-related protein kinase 1 (SnRK1) is involved in primary C/N-nutrient signal mediation via the transcriptional regulation of C/N-regulatory kinases. We also identified a leucine-rich repeat receptor-like kinase with extracellular malectin-like domain, named as LMK1, which was shown to possess cell death induction activity in plant leaves. These results provide important insight into the C/N-nutrient signaling pathways connecting nutrition stress to various cellular and physiological processes in plants.