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TitleThe identification of XPR1 as a voltage- and phosphate-activated phosphate-permeable ion channel.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 4519, Year 2025
Publish dateMay 15, 2025
AuthorsHongjiang Wu / Liang Sun / Tong Huo / Theodore G Wensel / Frank T Horrigan / Zhao Wang /
PubMed AbstractMaintaining a balance of inorganic phosphate (Pi) is vital for cellular functionality. Proper phosphate levels are managed through Pi import and export; and the processes governing Pi export remain ...Maintaining a balance of inorganic phosphate (Pi) is vital for cellular functionality. Proper phosphate levels are managed through Pi import and export; and the processes governing Pi export remain the least understood. Xenotropic and Polytropic retrovirus Receptor 1 (XPR1) has been identified as the only known Pi export protein in mammals. In this study, we introduce the cryogenic electron microscopy structure of human XPR1 (hXPR1), unveiling a structural arrangement distinct from that of any known ion transporter. Our structural results suggest that hXPR1 may operate as an ion channel, a hypothesis supported by patch clamp recordings revealing hXPR1's voltage- and Pi-dependent activity and large unitary conductance. Further analyses, including the structure of hXPR1 in presence of Pi, and mutagenesis studies at one of the putative Pi binding sites, lead us to propose a plausible ion permeation pathway. Together, our results provide novel perspectives on the Pi transport mechanism of XPR1.
External linksNat Commun / PubMed:40374661 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.45 Å
Structure data

45656

9ckz

EMDB-45656: Cryo-EM map of human XPR1 in apo state
PDB-9ckz: Cryo-EM structure of human XPR1 in apo state
Method: EM (single particle) / Resolution: 3.45 Å

45657

9cl0

EMDB-45657: Cryo-EM map of human XPR1 in presence of inorganic phosphate and phytic acid
PDB-9cl0: Cryo-EM structure of human XPR1 in presence of inorganic phosphate and phytic acid
Method: EM (single particle) / Resolution: 2.3 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Ion channel / phosphate transport

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