title: EDR2 negatively regulates salicylic acid-based defenses and cell death during powdery mildew infections of Arabidopsis thaliana.
abstract: BACKGROUND
  The hypersensitive necrosis response (HR) of resistant plants to avirulent pathogens is a form of programmed cell death in which the plant sacrifices a few cells under attack, restricting pathogen growth into adjacent healthy tissues. In spite of the importance of this defense response, relatively little is known about the plant components that execute the cell death program or about its regulation in response to pathogen attack.
  
  
  RESULTS
  We isolated the edr2-6 mutant, an allele of the previously described edr2 mutants. We found that edr2-6 exhibited an exaggerated chlorosis and necrosis response to attack by three pathogens, two powdery mildew and one downy mildew species, but not in response to abiotic stresses or attack by the bacterial leaf speck pathogen. The chlorosis and necrosis did not spread beyond inoculated sites suggesting that EDR2 limits the initiation of cell death rather than its spread. The pathogen-induced chlorosis and necrosis of edr2-6 was correlated with a stimulation of the salicylic acid defense pathway and was suppressed in mutants deficient in salicylic acid signaling. EDR2 encodes a novel protein with a pleckstrin homology and a StAR transfer (START) domain as well as a plant-specific domain of unknown function, DUF1336. The pleckstrin homology domain binds to phosphatidylinositol-4-phosphate in vitro and an EDR2:HA:GFP protein localizes to endoplasmic reticulum, plasma membrane and endosomes.
  
  
  CONCLUSIONS
  EDR2 acts as a negative regulator of cell death, specifically the cell death elicited by pathogen attack and mediated by the salicylic acid defense pathway. Phosphatidylinositol-4-phosphate may have a role in limiting cell death via its effect on EDR2. This role in cell death may be indirect, by helping to target EDR2 to the appropriate membrane, or it may play a more direct role.
authors.affiliation: Carnegie Institution, Department of Plant Biology, Stanford, CA 94305, USA. sonja.vorwerk@t-online.de
authors.forename: Sonja
authors.initials: S
authors.lastname: Vorwerk
authors.forename: Celine
authors.initials: C
authors.lastname: Schiff
authors.forename: Marjorie
authors.initials: M
authors.lastname: Santamaria
authors.forename: Serry
authors.initials: S
authors.lastname: Koh
authors.forename: Marc
authors.initials: M
authors.lastname: Nishimura
authors.forename: John
authors.initials: J
authors.lastname: Vogel
authors.forename: Chris
authors.initials: C
authors.lastname: Somerville
authors.forename: Shauna
authors.initials: S
authors.lastname: Somerville
mesh_terms: D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D001203:Ascomycota / Q000472:pathogenicity*; D016923:Cell Death / Q000235:genetics / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D005936:Glucans / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D018613:Microscopy, Confocal; D009154:Mutation; D010641:Phenotype; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism; D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D030821:Plants, Genetically Modified; D011485:Protein Binding; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D020156:Salicylic Acid / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; D005936:Glucans; D018129:Phosphatidylinositol Phosphates; D011993:Recombinant Fusion Proteins; C037178:phosphatidylinositol 4-phosphate; D049452:Green Fluorescent Proteins; C048306:callose; D006861:Hydrogen Peroxide; D020156:Salicylic Acid