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

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

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 70(2019), 21 vom: 18. Nov., Seite 6375-6388
1. Verfasser: Xu, Guoyun (VerfasserIn)
Weitere Verfasser: Chen, Weijun, Song, Limei, Chen, Qiansi, Zhang, Hui, Liao, Hongdong, Zhao, Guoqiang, Lin, Fucheng, Zhou, Huina, Yu, Feng
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana 14-3-3 protein ATL6 E3 ubiquitin ligase FERONIA RALF1 carbon/nitrogen response phosphorylation mehr... 14-3-3 Proteins Arabidopsis Proteins Peptide Hormones RALF1 protein, Arabidopsis Carbon 7440-44-0 AT3G05200 protein, Arabidopsis EC 2.3.2.27 Ubiquitin-Protein Ligases FERONIA receptor like kinase, Arabidopsis EC 2.7.- Phosphotransferases Nitrogen N762921K75
Beschreibung
Zusammenfassung:© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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
Beschreibung:Date Completed 10.08.2020
Date Revised 08.10.2020
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erz378