FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio-Reference-Cited by-全球学者库

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

Published:2019-08-21 Issue:21 Volume:70 Page:6375-6388
ISSN:0022-0957
Container-title:Journal of Experimental Botany
language:en
Short-container-title:

Author:

Xu Guoyun¹^ORCID,Chen Weijun²,Song Limei²,Chen Qiansi¹,Zhang Hui¹,Liao Hongdong²,Zhao Guoqiang³,Lin Fucheng⁴,Zhou Huina¹^ORCID,Yu Feng²⁵¹^ORCID

Affiliation:

1. Zhengzhou Tobacco Research Institute of China National Tobacco Corporation, Zhengzhou, PR China

2. State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, and Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation Hunan University, Changsha, PR China

3. School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, PR China

4. State Key Laboratory for Rice Biology, Biotechnology Institute, Zhejiang University, Hangzhou, PR China

5. State Key Laboratory of Hybrid Rice, Hunan Hybrid Rice Research Center, Changsha, PR China

Abstract

This study reveals a novel regulatory mechanism that links the versatile receptor kinase FERONIA with plant C/N responses.

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Physiology

Link

http://academic.oup.com/jxb/advance-article-pdf/doi/10.1093/jxb/erz378/30063108/erz378.pdf

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