ArticleNature communications2025
Structural insights into the mechanism of phosphate recognition and transport by XPR1.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Untangling Inositol (Pyro)Phosphate Biology Through Emerging Technologies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026Article
- Primary Brain Calcification Associated with a Novel XPR1 In-Frame Deletion: Clinical Characterization and Insights into Cerebellar and Basal Ganglia Contributions.Cerebellum (London, England) · 2026Article
- Structural and dynamic insights into SPDT for phosphorus allocation in rice.Science China. Life sciences · 2026Article
- Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.Cell discovery · 2026Article
- Short-term dietary deoxynivalenol exposure negatively affects performance, intestinal and reproductive functions in laying hens.Scientific reports · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- XPR1 regulates fetal liver macrophage development, identity, and pyrenocyte clearance.The Journal of experimental medicine · 2026Article
- Sustainable Greenhouse Tomato Production: Benefits of Inoculation With Arbuscular Mycorrhizal Fungi Under Low Nitrogen and Phosphorus Conditions.Plant-environment interactions (Hoboken, N.J.) · 2025Article
- The SLC-ome of membrane transport: From molecular discovery to physiology and clinical applications.Physiological reviews · 2025Review
- Structure and function of human XPR1 in phosphate export.Nature communications · 2025Article
- Transport and InsPNature communications · 2025Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
XPR1 is the sole protein known to transport inorganic phosphate (Pi) out of cells, a function conserved across species from yeast to mammals. Human XPR1 variants lead to cerebral calcium-phosphate deposition and primary familial brain calcification (PFBC), a hereditary neurodegenerative disorder. Here, we present the cryo-EM structure of human XPR1 in both its Pi-unbound and various Pi-bound states. XPR1 features 10 transmembrane α-helices forming an ion channel-like structure, with multiple Pi recognition sites along the channel. Pathogenic mutations in two arginine residues, which line the translocation channel, disrupt Pi transport. Molecular dynamics simulations reveal that Pi ion undergoes a stepwise transition through the sequential recognition sites during the transport process. Together with functional analyses, our results suggest that this sequential arrangement allows XPR1 to facilitate Pi ion passage via a "relay" process, and they establish a framework for the interpretation of disease-related mutations and for the development of future therapeutics.
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