Claim · model-written summary
The Pst effector PstCFEM2 competitively binds the C-terminus of TaHA2, disrupting TaCIPK9-mediated phosphorylation and relieving autoinhibition.
- Taxon
- wheat
Triticum aestivumt0 - Interactor
- Pste0pathogen
- Gene
- PstCFEM2e0
- Outcome
- TaCIPK9-mediated phosphorylatione0
- Direction
- disruptinge0
Not reportedMaterialCompoundOrgan / stageSecond interactorSecond interactor roleTreatmentComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the CFEM (common in fungal extracellular membrane)-containing Pst effector PstCFEM2 competitively binds to the C-terminus of TaHA2, disrupting TaCIPK9-mediated phosphorylation and relieving autoinhibition”
t0“wheat susceptibility”
Title
Yanqin Zhang; Shuangyuan Guo; Longhui Yu; et al. The Plant Cell 2026. doi:10.1093/plcell/koag021
Other claims from this paper (6)
- Mechanism Wheat PM H+-ATPase TaHA2 was identified as a key regulator of apoplastic pH and defense responses to Pst infection.
- Intervention effect Overexpression of TaHA2 exacerbated apoplastic acidification and susceptibility to Pst.
- Intervention effect CRISPR-Cas9-mediated inactivation of TaHA2 in wheat conferred broad-spectrum resistance against multiple rust pathogens.
- Intervention effect CRISPR-Cas9 inactivation of TaHA2 in wheat did not compromise agronomic traits.
- Mechanism TaCIPK9 phosphorylates TaHA2 at Ser-933, triggering intramolecular interactions that suppress TaHA2 activity.
- Mechanism Effector-driven activation of TaHA2 amplifies apoplastic acidification and stomatal opening, ultimately dampening plant immunity.