ArticleNature communications2016
Structural basis for Mep2 ammonium transceptor activation by phosphorylation.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 63 citations in OpenAlex.
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- Regulation of organic anion transporting polypeptide 1B1 transport function by concurrent phosphorylation and lysine-acetylation: A novel posttranslational regulation mechanism.Molecular pharmacology · 2025Article
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- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Progress of Molecular Display Technology UsingMicroorganisms · 2023Review
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Functional Characterization of Sugar Transporter CRT1 Reveals Differential Roles of Its C-Terminal Region in Sugar Transport and Cellulase Induction in Trichoderma reesei.Microbiology spectrum · 2022Article
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- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Role of protein phosphatases in the regulation of nitrogen nutrition in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- A conformational change in the N terminus of SLC38A9 signals mTORC1 activation.Structure (London, England : 1993) · 2021Article
- Cation Transporters ofBiomolecules · 2021Review
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- A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mep2 proteins are fungal transceptors that play an important role as ammonium sensors in fungal development. Mep2 activity is tightly regulated by phosphorylation, but how this is achieved at the molecular level is not clear. Here we report X-ray crystal structures of the Mep2 orthologues from Saccharomyces cerevisiae and Candida albicans and show that under nitrogen-sufficient conditions the transporters are not phosphorylated and present in closed, inactive conformations. Relative to the open bacterial ammonium transporters, non-phosphorylated Mep2 exhibits shifts in cytoplasmic loops and the C-terminal region (CTR) to occlude the cytoplasmic exit of the channel and to interact with His2 of the twin-His motif. The phosphorylation site in the CTR is solvent accessible and located in a negatively charged pocket ∼30 Å away from the channel exit. The crystal structure of phosphorylation-mimicking Mep2 variants from C. albicans show large conformational changes in a conserved and functionally important region of the CTR. The results allow us to propose a model for regulation of eukaryotic ammonium transport by phosphorylation.
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