Evidence map›Paper›PMID 39814721›Full record

ArticleNature communications2025

Structural basis of phosphate export by human XPR1.

Qixian He, Ran Zhang, Sandrine Tury, Valérie Courgnaud, Fenglian Liu, Jean-Luc Battini, Baobin Li, Qingfeng Chen

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Review
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  10. Review
  11. Review
  12. Article
  13. Enabling Technologies for the Dissection of Inositol Pyrophosphate Physiology.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Qixian He *Center for Life Sciences, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, School of Life Sciences, Yunnan University, Kunming, China.
Ran Zhang *Department of Anesthesiology, Zhongshan Hospital, Institute for Translational Brain Research, State Key Laboratory of Medical Neurobiology, MOE Frontiers Center for Brain Science, Fudan University, Shanghai, China.
Sandrine Tury *Institut de Recherche en Infectiologie de Montpellier IRIM - CNRS UMR 9004, Université Montpellier, Montpellier, France.ORCID http://orcid.org/0000-0001-9291-734X
Valérie CourgnaudInstitut de Génétique Moléculaire de Montpellier IGMM - CNRS UMR 5535, Université Montpellier, Montpellier, France.ORCID http://orcid.org/0000-0003-1000-0322
Fenglian LiuCenter for Life Sciences, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, School of Life Sciences, Yunnan University, Kunming, China.ORCID http://orcid.org/0009-0002-6960-2520
Jean-Luc BattiniInstitut de Recherche en Infectiologie de Montpellier IRIM - CNRS UMR 9004, Université Montpellier, Montpellier, France. jean-luc.battini@irim.cnrs.fr.ORCID http://orcid.org/0000-0002-5884-9934
Baobin LiDepartment of Anesthesiology, Zhongshan Hospital, Institute for Translational Brain Research, State Key Laboratory of Medical Neurobiology, MOE Frontiers Center for Brain Science, Fudan University, Shanghai, China. libaobin@fudan.edu.cn.ORCID http://orcid.org/0000-0002-4560-4575
Qingfeng ChenCenter for Life Sciences, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, School of Life Sciences, Yunnan University, Kunming, China. qingfengchen@ynu.edu.cn.ORCID http://orcid.org/0000-0001-9526-0806

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32071202 and 32271012National Natural Science Foundation of China (National Science Foundation of China) 32371261
6 · The paper itself

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.

Indexed as

PhosphatesReceptors, Cytoplasmic and NuclearReceptors, G-Protein-CoupledBinding SitesCryoelectron MicroscopyHumansModels, MolecularProtein BindingProtein DomainsProtein MultimerizationXenotropic and Polytropic Retrovirus ReceptorPhosphatesReceptors, Cytoplasmic and NuclearReceptors, G-Protein-CoupledXenotropic and Polytropic Retrovirus ReceptorXPR1 protein, human

Identifiers

PMID39814721
PMCPMC11736019

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.