| Literature DB >> 27930296 |
Changqing Du1, Xiushan Li1, Jia Chen1, Weijun Chen1, Bin Li1, Chiyu Li1, Long Wang1, Jianglin Li1, Xiaoying Zhao1, Jianzhong Lin1, Xuanming Liu2, Sheng Luan3, Feng Yu2.
Abstract
A number of hormones work together to control plant cell growth. Rapid Alkalinization Factor 1 (RALF1), a plant-derived small regulatory peptide, inhibits cell elongation through suppression of rhizosphere acidification in plants. Although a receptor-like kinase, FERONIA (FER), has been shown to act as a receptor for RALF1, the signaling mechanism remains unknown. In this study, we identified a receptor-like cytoplasmic kinase (RPM1-induced protein kinase, RIPK), a plasma membrane-associated member of the RLCK-VII subfamily, that is recruited to the receptor complex through interacting with FER in response to RALF1. RALF1 triggers the phosphorylation of both FER and RIPK in a mutually dependent manner. Genetic analysis of the fer-4 and ripk mutants reveals RIPK, as well as FER, to be required for RALF1 response in roots. The RALF1-FER-RIPK interactions may thus represent a mechanism for peptide signaling in plants.Entities:
Keywords: feronia; phosphorylation; plant hormone
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Year: 2016 PMID： 27930296 PMCID： PMC5187724 DOI： 10.1073/pnas.1609626113
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205