Claim · model-written summary
The EDR2 pleckstrin homology domain binds phosphatidylinositol-4-phosphate in vitro.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Compound
- phosphatidylinositol-4-phosphatee6
- Outcome
- bindse6
- Setting
- in vitroe6
Not reportedMaterialGeneOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e6“The pleckstrin homology domain binds to phosphatidylinositol-4-phosphate in vitro”
t0“Arabidopsis thaliana”
Title
Sonja Vorwerk; Celine Schiff; Marjorie Santamaria; et al. BMC Plant Biology 2007. doi:10.1186/1471-2229-7-35
Other claims from this paper (8)
- Association edr2-6 showed an exaggerated chlorosis and necrosis response to attack by two powdery mildew species and one downy mildew species.
- Observation edr2-6 showed no exaggerated chlorosis and necrosis response to abiotic stresses or to the bacterial leaf speck pathogen.
- Mechanism Chlorosis and necrosis did not spread beyond inoculated sites, suggesting that EDR2 limits the initiation of cell death rather than its spread.
- Association Pathogen-induced chlorosis and necrosis of edr2-6 was correlated with stimulation of the salicylic acid defense pathway.
- Association Pathogen-induced chlorosis and necrosis of edr2-6 was suppressed in mutants deficient in salicylic acid signaling.
- Observation EDR2 encodes a novel protein with a pleckstrin homology domain, a StAR transfer (START) domain and a plant-specific domain of unknown function, DUF1336.
- Observation The EDR2:HA:GFP protein localizes to the endoplasmic reticulum, plasma membrane and endosomes.
- Mechanism 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.