ArticleNature communications2025
Structural basis of phosphate export by human 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 13 papers.
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Who cites it
13 citing papers in PubMed.
- Review
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
- The PHO1 protein family in phosphate export and beyond.Plant physiology · 2026Review
- Citrulline drives age-related lipid deposition for healthspan.Nature communications · 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 insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.Cell discovery · 2026Article
- Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.Nature communications · 2026Article
- XPR1 regulates fetal liver macrophage development, identity, and pyrenocyte clearance.The Journal of experimental medicine · 2026Article
- Role of Inositol Hexakisphosphate Kinases in Vascular Smooth Muscle Cell Calcification.International journal of molecular sciences · 2026Article
- Multilayered Regulation of Fungal Phosphate Metabolism: From Molecular Mechanisms to Ecological Roles in the Global Phosphorus Cycle.Life (Basel, Switzerland) · 2025Review
- 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
- Enabling Technologies for the Dissection of Inositol Pyrophosphate Physiology.Methods in molecular biology (Clifton, N.J.) · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
Phosphorus in crucial for all living organisms. In vertebrate, cellular phosphate homeostasis is partly controlled by XPR1, a poorly characterized inositol pyrophosphate-dependent phosphate exporter. Here, we report the cryo-EM structure of human XPR1, which forms a loose dimer with 10 transmembrane helices (TM) in each protomer. The structure consists of a scaffold domain (TM1, TM3-4) and a core domain (TM2, TM5-10) structurally related to ion-translocating rhodopsins. Bound phosphate is observed in a tunnel within the core domain at a narrow point that separates the tunnel into intracellular and extracellular vestibules. This site contains a cluster of basic residues that coordinate phosphate and a conserved W573 essential for export function. Loss of inositol pyrophosphate binding is accompanied by structural movements in TM9 and the W573 sidechain, closing the extracellular vestibule and blocking phosphate export. These findings provide insight into XPR1 mechanism and pave the way for further in-depth XPR1 studies.
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