FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio.

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  • Additional Information
    • Source:
      Publisher: Oxford University Press Country of Publication: England NLM ID: 9882906 Publication Model: Print Cited Medium: Internet ISSN: 1460-2431 (Electronic) Linking ISSN: 00220957 NLM ISO Abbreviation: J Exp Bot Subsets: MEDLINE
    • Publication Information:
      Original Publication: Oxford, UK : Oxford University Press,
    • Subject Terms:
      14-3-3 Proteins/*metabolism ; Arabidopsis Proteins/*metabolism ; Carbon/*pharmacology ; Nitrogen/*pharmacology ; Phosphotransferases/*metabolism ; Ubiquitin-Protein Ligases/*metabolism; Amino Acid Sequence ; Arabidopsis Proteins/chemistry ; Models, Biological ; Peptide Hormones/metabolism ; Phosphorylation/drug effects ; Phosphotransferases/chemistry ; Protein Binding/drug effects ; Ubiquitin-Protein Ligases/chemistry
    • Abstract:
      The ratio between carbon (C) and nitrogen (N) utilization must be precisely coordinated to enable plant growth. Although numerous physiological studies have examined carbon/nitrogen (C/N) ratios, the mechanisms of sensing the C/N balance and C/N signaling remain elusive. Here, we report that a mutation of FERONIA (FER), a receptor kinase that plays versatile roles in plant cell growth and stress responses, caused hypersensitivity to a high C/N ratio in Arabidopsis. In contrast, FER-overexpressing plants displayed more resistant phenotypes. FER can interact with and phosphorylate ATL6, an E3 ubiquitin ligase that has been shown to regulate plant C/N responses. FER-mediated ATL6 phosphorylation enhanced the interaction between ATL6 and its previously identified target 14-3-3 proteins, thus decreasing 14-3-3 protein levels, leading to an increased insensitivity to high C/N ratios. Further analyses showed that the rapid alkalinization factor peptide (RALF1), which is a ligand of FER, also influenced the stability of 14-3-3 proteins via a FER-ATL6-mediated pathway. These findings reveal a novel regulatory mechanism that links the RALF1/FER-ATL6 pathway to whole-plant C/N responses and growth.
      (© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.)
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    • Contributed Indexing:
      Keywords: Arabidopsis thaliana; 14-3-3 protein; ATL6; E3 ubiquitin ligase; FERONIA; RALF1; carbon/nitrogen response; phosphorylation
    • Accession Number:
      0 (14-3-3 Proteins)
      0 (Arabidopsis Proteins)
      0 (Peptide Hormones)
      0 (RALF1 protein, Arabidopsis)
      7440-44-0 (Carbon)
      EC 2.3.2.27 (AT3G05200 protein, Arabidopsis)
      EC 2.3.2.27 (Ubiquitin-Protein Ligases)
      EC 2.7.- (FERONIA receptor like kinase, Arabidopsis)
      EC 2.7.- (Phosphotransferases)
      N762921K75 (Nitrogen)
    • Publication Date:
      Date Created: 20190822 Date Completed: 20200810 Latest Revision: 20201008
    • Publication Date:
      20221213
    • Accession Number:
      PMC6859809
    • Accession Number:
      10.1093/jxb/erz378
    • Accession Number:
      31433471