ArticleScience advances2024
How sensor Amt-like proteins integrate ammonium signals.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Preparation of Plasma Membrane Vesicles, Lysosomes, Proteoliposomes and Alternative Sample Types for SSM-Based Electrophysiology.Methods in molecular biology (Clifton, N.J.) · 2026Article
- High-Sensitivity, Low Detection Limit, and Fast Ammonia Detection of Ag-NiFeNanomaterials (Basel, Switzerland) · 2025Article
- Structural and functional diversity of sensor domains in bacterial transmembrane receptors.Trends in microbiology · 2025Review
- Extensive paralogism in the environmental pangenome: a key factor in the ecological success of natural SAR11 populations.Microbiome · 2025Article
- Functional crosstalk between nitrate and ammonium transporters in N acquisition and pH homeostasis.Frontiers in plant science · 2025Review
- Nitrate and ammonium, the yin and yang of nitrogen uptake: a time-course transcriptomic study in rice.Frontiers in plant science · 2024Article
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Authors and funding
9 authors.
Funding
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Abstract
Unlike aquaporins or potassium channels, ammonium transporters (Amts) uniquely discriminate ammonium from potassium and water. This feature has certainly contributed to their repurposing as ammonium receptors during evolution. Here, we describe the ammonium receptor Sd-Amt1, where an Amt module connects to a cytoplasmic diguanylate cyclase transducer module via an HAMP domain. Structures of the protein with and without bound ammonium were determined to 1.7- and 1.9-Ångstrom resolution, depicting the ON and OFF states of the receptor and confirming the presence of a binding site for two ammonium cations that is pivotal for signal perception and receptor activation. The transducer domain was disordered in the crystals, and an AlphaFold2 prediction suggests that the helices linking both domains are flexible. While the sensor domain retains the trimeric fold formed by all Amt family members, the HAMP domains interact as pairs and serve to dimerize the transducer domain upon activation.
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