<<< Full experiment listing

PXD025597

PXD025597 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleALLOSTERIC ACTIVATION OF A PLANT IMMUNE RECEPTOR KINASE COMPLEX
DescriptionReceptor kinases (RKs) play fundamental roles in extracellular sensing to regulate development and stress responses across kingdoms. In plants, leucine-rich repeat receptor kinases (LRR-RKs) function primarily as peptide receptors that regulate myriad aspects of plant development and response to external stimuli. Extensive phosphorylation of LRR-RK cytoplasmic domains is among the earliest detectable responses following ligand perception, and reciprocal transphosphorylation between a receptor and its co-receptor is proposed to activate the receptor complex. Originally conceived 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 RK, we set out to understand the steps critical for activating RK complexes. The EFR cytoplasmic domain is an active protein kinase in vitro and is phosphorylated in a ligand-dependent manner in vivo. Nevertheless, catalytically deficient EFR variants are functional in anti-bacterial immunity. These results reveal a non-catalytic role for the EFR cytoplasmic domain 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-RK complexes with RD- versus non-RD-type 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-type protein kinase may be activated by an allosteric mechanism triggered by activation segment phosphorylation and possibly involving conformational changes of the protein kinase domain of the ligand-binding receptor.
HostingRepositoryPRIDE
AnnounceDate2021-10-27
AnnouncementXMLSubmission_2021-10-26_22:36:48.931.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD025597
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterFRank Menke
SpeciesList scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationListphosphorylated residue
InstrumentLTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-04-23 06:21:07ID requested
12021-10-26 22:36:49announced
Publication List
Bender KW, Couto D, Kadota Y, Macho AP, Sklenar J, Derbyshire P, Bjornson M, DeFalco TA, Petriello A, Font Farre M, Schwessinger B, Ntoukakis V, Stransfeld L, Jones AME, Menke FLH, Zipfel C, Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling. Proc Natl Acad Sci U S A, 118(38):(2021) [pubmed]
Keyword List
submitter keyword: receptor kinase, protein kinase, phosphorylation, pattern recognition receptor, innate immunity.
Contact List
Frank L.H. Menke
contact affiliationThe Sainsbury Laboratory
contact emailfrank.menke@tsl.ac.uk
lab head
FRank Menke
contact affiliationthe Sainsbury laboratory
contact emailFrank.Menke@tsl.ac.uk
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/10/PXD025597
PRIDE project URI
Repository Record List
[ + ]