title: A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.
abstract: Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.
authors.affiliation: The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, UK.
authors.forename: Alberto P
authors.initials: AP
authors.lastname: Macho
authors.forename: Benjamin
authors.initials: B
authors.lastname: Schwessinger
authors.forename: Vardis
authors.initials: V
authors.lastname: Ntoukakis
authors.forename: Alexandre
authors.initials: A
authors.lastname: Brutus
authors.forename: Cécile
authors.initials: C
authors.lastname: Segonzac
authors.forename: Sonali
authors.initials: S
authors.lastname: Roy
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Kadota
authors.forename: Man-Ho
authors.initials: MH
authors.lastname: Oh
authors.forename: Jan
authors.initials: J
authors.lastname: Sklenar
authors.forename: Paul
authors.initials: P
authors.lastname: Derbyshire
authors.forename: Rosa
authors.initials: R
authors.lastname: Lozano-Durán
authors.forename: Frederikke Gro
authors.initials: FG
authors.lastname: Malinovsky
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Monaghan
authors.forename: Frank L
authors.initials: FL
authors.lastname: Menke
authors.forename: Steven C
authors.initials: SC
authors.lastname: Huber
authors.forename: Sheng Yang
authors.initials: SY
authors.lastname: He
authors.forename: Cyril
authors.initials: C
authors.lastname: Zipfel
mesh_terms: D017360:Arabidopsis / Q000276:immunology* / Q000382:microbiology*; D029681:Arabidopsis Proteins / Q000819:agonists / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism / Q000494:pharmacology; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D044224:Pseudomonas syringae / Q000201:enzymology / Q000472:pathogenicity*; D051192:Receptors, Pattern Recognition / Q000819:agonists / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; C545106:EFR protein, Arabidopsis; D010455:Peptides; D051192:Receptors, Pattern Recognition; D014443:Tyrosine; D017027:Protein Tyrosine Phosphatases; D010444:Peptide Elongation Factor Tu