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Protein Phosphorylation Dynamics Under Carbon/Nitrogen-Nutrient Stress and Identification of a Cell Death-Related Receptor-Like Kinase in Arabidopsis

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Title: Protein Phosphorylation Dynamics Under Carbon/Nitrogen-Nutrient Stress and Identification of a Cell Death-Related Receptor-Like Kinase in Arabidopsis
Authors: Li, Xingwen Browse this author
Sanagi, Miho Browse this author
Lu, Yu Browse this author
Nomura, Yuko Browse this author
Stolze, Sara Christina Browse this author
Yasuda, Shigetaka Browse this author
Saijo, Yusuke Browse this author
Schulze, Waltraud X. Browse this author
Feil, Regina Browse this author
Stitt, Mark Browse this author
Lunn, John E. Browse this author
Nakagami, Hirofumi Browse this author
Sato, Takeo Browse this author
Yamaguchi, Junji Browse this author →KAKEN DB
Keywords: sugar
nitrogen
phosphorylation
kinase
SnRK1
receptor-like kinase
metabolism
cell death
Issue Date: 3-Apr-2020
Publisher: Frontiers Media
Journal Title: Frontiers in plant science
Volume: 11
Start Page: 377
Publisher DOI: 10.3389/fpls.2020.00377
Abstract: 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.
Rights: https://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/78408
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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