{
  "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.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "Bangguo He",
      "orcid": "0009-0008-0563-704X"
    },
    {
      "name": "Ting Bai",
      "orcid": "0000-0001-8216-089X"
    },
    {
      "name": "Liyang Wang",
      "orcid": "0009-0008-9726-2563"
    },
    {
      "name": "Shuai Zhang",
      "orcid": "0009-0008-4002-6455"
    },
    {
      "name": "Wei Ying"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/9db24jjtnahec.bib",
  "cited_by": 0,
  "doi": "10.1038/s41467-026-78457-1",
  "fulltext_url": null,
  "id": "9db24jjtnahec",
  "issns": [
    "2041-1723"
  ],
  "landing_url": "https://www.nature.com/articles/s41467-026-78457-1",
  "language": null,
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1110|Plant nutrient uptake and metabolism"
    ]
  ],
  "openalex": "W7221347490",
  "pdf_url": "https://www.nature.com/articles/s41467-026-78457-1_reference.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-10",
  "publisher": "Springer Science and Business Media LLC",
  "ris": "https://research.draconitic.com/paper/9db24jjtnahec.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:38Z",
      "native_id": "10.1038/s41467-026-78457-1",
      "source": "crossref",
      "url": "https://www.nature.com/articles/s41467-026-78457-1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:1110|Plant nutrient uptake and metabolism",
      "subfield": "plant-biology"
    }
  ],
  "title": "Structural basis of ammonium transport and coordinated regulation of AMT1;1 in Arabidopsis thaliana",
  "title_text": "Structural basis of ammonium transport and coordinated regulation of AMT1;1 in Arabidopsis thaliana",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:38Z",
  "url": "https://research.draconitic.com/paper/9db24jjtnahec",
  "venue": "Nature Communications",
  "versions": []
}