气候变化领域集成服务门户(CCPortal): Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling

CCPortal

DOI	10.1073/pnas.2108242118
	Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling
	Bender K.W.; Couto D.; Kadota Y.; Macho A.P.; Sklenar J.; Derbyshire P.; Bjornson M.; DeFalco T.A.; Petriello A.; Farre M.F.; Schwessinger B.; Ntoukakis V.; Stransfeld L.; Jones A.M.E.; Menke F.L.H.; Zipfel C.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:38
英文摘要	Receptor kinases (RKs) are fundamental for extracellular sensing and regulate development and stress responses across kingdoms. In plants, leucine-rich repeat receptor kinases (LRR-RKs) are primarily peptide receptors that regulate responses to myriad internal and external stimuli. Phosphorylation of LRR-RK cytoplasmic domains is among the earliest responses following ligand perception, and reciprocal transphosphorylation between a receptor and its coreceptor is thought to activate the receptor complex. Originally proposed based on characterization of the brassinosteroid receptor, the prevalence of complex activation via reciprocal transphosphorylation across the plant RK family has not been tested. Using the LRR-RK ELONGATION FACTOR TU RECEPTOR (EFR) as a model, we set out to understand the steps critical for activating RK complexes. While the EFR cytoplasmic domain is an active protein kinase in vitro and is phosphorylated in a ligand-dependent manner in vivo, catalytically deficient EFR variants are functional in antibacterial immunity. These results reveal a noncatalytic role for EFR in triggering immune signaling and indicate that reciprocal transphoshorylation is not a ubiquitous requirement for LRR-RK complex activation. Rather, our analysis of EFR along with a detailed survey of the literature suggests a distinction between LRR-RKs with RD- versus non-RD protein kinase domains. Based on newly identified phosphorylation sites that regulate the activation state of the EFR complex in vivo, we propose that LRR-RK complexes containing a non-RD protein kinase may be regulated by phosphorylation-dependent conformational changes of the ligand-binding receptor, which could initiate signaling either allosterically or through driving the dissociation of negative regulators of the complex. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Phosphorylation; Receptor kinase; Signaling
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/238794
作者单位	Institute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, 8008, Switzerland; Sainsbury Laboratory, University of East Anglia, Norwich, NR4 7UH, United Kingdom
推荐引用方式 GB/T 7714	Bender K.W.,Couto D.,Kadota Y.,et al. Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling[J],2021,118(38).
APA	Bender K.W..,Couto D..,Kadota Y..,Macho A.P..,Sklenar J..,...&Zipfel C..(2021).Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America,118(38).
MLA	Bender K.W.,et al."Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling".Proceedings of the National Academy of Sciences of the United States of America 118.38(2021).