Claim · model-written summary
The arginine-to-glutamine mutation in XXT N-termini significantly reduced the strength of the interaction with AtSar1.
- Taxon
- Arabidopsis
Arabidopsist0 - Treatment
- mutation of the arginine to glutamine residues of di-arginine motifse0
- Gene
- XXTse0
- Outcome
- strength of the interaction with AtSar1e1
- Direction
- reducede1
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis”
e0“The mutation of the arginine to glutamine residues of di-arginine motifs in the N-termini of XXTs”
e1“significantly reduced the strength of the interaction with AtSar1”
Title
Ning Zhang; Jordan D. Julian; Olga A. Zabotina Plants 2026. doi:10.3390/plants15050822
Other claims from this paper (7)
- Observation XXTs interact with AtSar1 in the COPII complex.
- Observation XXTs do not interact with AtSec24.
- Intervention effect Mutating arginine to glutamine in the di-arginine motifs of the XXT N-termini caused protein mislocalization.
- Intervention effect The mutations caused 90% of XXTs to remain in the ER or localize to small non-Golgi compartments.
- Intervention effect Mislocalization of the mutated XXTs significantly suppressed recovery of xyloglucan biosynthesis in the xxt1xxt2 and xxt3xxt4xxt5 mutants.
- Intervention effect The mislocalized XXTs failed to restore the root phenotypes of the mutants to normal.
- Mechanism The authors conclude that di-arginine motifs play a critical role in the cargo-AtSar1 interaction.