{
  "abstract": "Ammonium (NH4+) uptake and transport in plants are mediated by ammonium transporters (AMTs), which are tightly regulated by phosphorylation to prevent excess ammonium influx and toxic accumulation. However, the mechanism of phosphorylation-mediated inactivation is unique and remains unclear. Here, we report cryo-EM structures of the rice (Oryza sativa) ammonium transporter OsAMT1;1 in its wild-type and phosphomimetic variant T452D states. OsAMT1;1 forms a stable homotrimer, with conserved motifs affirming a shared transport mechanism within the AMT/MEP/Rh superfamily. Our structural analysis reveals that T452D phosphomimetic stabilizes an intracellular salt-bridge network and maintains the channel in a closed state, in which the ICL5 loop positions the hydrophobic plug residue Leu360 near the cytoplasmic exit to occlude the channel exit and abolish complementation capacity. Our findings elucidate phosphorylation-induced inactivation mechanism for the plant AMT1 subfamily, providing a structural paradigm for the post-translational regulation of nutrient uptake.",
  "abstract_shown": true,
  "affiliations": [
    "CAS Center for Excellence in Molecular Plant Sciences"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "name": "F. Yu"
    },
    {
      "name": "X. Huang"
    },
    {
      "name": "S. Wang"
    },
    {
      "name": "N. An"
    },
    {
      "affs": [
        0
      ],
      "name": "P. Zhang"
    },
    {
      "name": "J. Huang"
    },
    {
      "affs": [
        0
      ],
      "name": "X. Zhang"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/cdw6nmtd04ayc.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.12.758405",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.758405v1.full",
  "id": "cdw6nmtd04ayc",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.758405v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "1110|Plant nutrient uptake and metabolism"
    ]
  ],
  "openalex": "W7221529886",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.758405v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-12",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/cdw6nmtd04ayc.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:27:24Z",
      "native_id": "10.64898/2026.10.12.758405",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.12.758405v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Structural basis for phosphorylation-induced inactivation of the rice ammonium transporter AMT1;1",
  "title_text": "Structural basis for phosphorylation-induced inactivation of the rice ammonium transporter AMT1;1",
  "type": "preprint",
  "updated_at": "2026-10-30T12:27:24Z",
  "url": "https://research.draconitic.com/paper/cdw6nmtd04ayc",
  "venue": "bioRxiv",
  "versions": []
}