Structural basis of ammonium transport and coordinated regulation of AMT1;1 in Arabidopsis thaliana
Abstract
Efficient ammonium uptake is essential for plant growth and nitrogen-use efficiency, yet the structural basis of ammonium transport and regulation in plant AMTs remains unclear. Here, we determined multiple cryo-electron microscopy structures of the Arabidopsis thaliana ammonium transporter AMT1;1 in apo, ammonium-bound, methylammonium-bound, low-pH and phosphomimetic states. These structures reveal a conserved ammonium conduction pathway comprising an aromatic recruitment vestibule, a Phe-gate/Twin-His-containing pore, and a polar intracellular exit region. We further identified a conserved extracellular N-terminal disulfide bond required for oligomer stability and transport activity, suggesting potential redox-dependent regulation. On the cytoplasmic side, phosphorylation modulates C-terminal interactions with intracellular loops, revealing an allosteric regulatory mechanism. Comparison with the bacterial ammonium-sensing protein Sd -Amt1 uncovers a conserved ammonium-recognition region in At AMT1;1 that contributes to transport activity but lacks the signaling module and ligand-dependent conformational switching observed in Sd -Amt1. Together, these findings provide structural insight into ammonium transport and coordinated regulation in plant AMT transporters.
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BibTeX
@article{he2026structural,
title = {{Structural basis of ammonium transport and coordinated regulation of AMT1;1 in Arabidopsis thaliana}},
author = {Bangguo He and Ting Bai and Liyang Wang and Shuai Zhang and Wei Ying},
journal = {Nature Communications},
year = {2026},
month = oct,
doi = {10.1038/s41467-026-78457-1},
url = {https://www.nature.com/articles/s41467-026-78457-1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Structural basis of ammonium transport and coordinated regulation of AMT1;1 in Arabidopsis thaliana
AU - Bangguo He
AU - Ting Bai
AU - Liyang Wang
AU - Shuai Zhang
AU - Wei Ying
PY - 2026
DA - 2026/10/10
JO - Nature Communications
DO - 10.1038/s41467-026-78457-1
UR - https://www.nature.com/articles/s41467-026-78457-1
AB - Efficient ammonium uptake is essential for plant growth and nitrogen-use efficiency, yet the structural basis of ammonium transport and regulation in plant AMTs remains unclear. Here, we determined multiple cryo-electron microscopy structures of the Arabidopsis thaliana ammonium transporter AMT1;1 in apo, ammonium-bound, methylammonium-bound, low-pH and phosphomimetic states. These structures reveal a conserved ammonium conduction pathway comprising an aromatic recruitment vestibule, a Phe-gate/Twin-His-containing pore, and a polar intracellular exit region. We further identified a conserved extracellular N-terminal disulfide bond required for oligomer stability and transport activity, suggesting potential redox-dependent regulation. On the cytoplasmic side, phosphorylation modulates C-terminal interactions with intracellular loops, revealing an allosteric regulatory mechanism. Comparison with the bacterial ammonium-sensing protein Sd -Amt1 uncovers a conserved ammonium-recognition region in At AMT1;1 that contributes to transport activity but lacks the signaling module and ligand-dependent conformational switching observed in Sd -Amt1. Together, these findings provide structural insight into ammonium transport and coordinated regulation in plant AMT transporters.
SN - 2041-1723
ER -