Evidence map›Paper›PMID 40128258›Full record

ArticleNature communications2025

Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate.

Peng Zuo, Weize Wang, Zonglin Dai, Jiye Zheng, Shang Yu, Guangxi Wang, Yue Yin, Ling Liang, Yuxin Yin

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Untangling Inositol (Pyro)Phosphate Biology Through Emerging Technologies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Article
  3. Review
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

9 authors.

Peng ZuoInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0002-5631-9534
Weize WangInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0001-7258-0356
Zonglin DaiInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0002-4005-1297
Jiye ZhengDepartment of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Shang YuDepartment of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0009-0002-2665-8882
Guangxi WangInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0002-4884-2990
Yue YinDepartment of Pharmacology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Ling LiangInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China. liangling@hsc.pku.edu.cn.ORCID http://orcid.org/0000-0002-3115-2563
Yuxin YinInstitute of Systems Biomedicine, Department of Pathology, Beijing Key Laboratory of Tumor Systems Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China. yinyuxin@hsc.pku.edu.cn.ORCID http://orcid.org/0000-0003-3646-8548

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32171224National Natural Science Foundation of China (National Science Foundation of China) 82030081
6 · The paper itself

Abstract

Inorganic phosphate (Pi) is essential for life, and its intracellular levels must be tightly regulated to avoid toxicity. XPR1, the sole known phosphate exporter, is critical for maintaining this balance. Here we report cryo-EM structures of the human XPR1-KIDINS220 complex in substrate-free closed and substrate-bound outward-open states, as well as an XPR1 mutant in a substrate-bound inward-facing state. In the presence of inositol hexaphosphate (InsP

Indexed as

Inositol PhosphatesMembrane ProteinsReceptors, G-Protein-CoupledCryoelectron MicroscopyHEK293 CellsHumansModels, MolecularPhosphatesPhytic AcidProtein BindingProtein ConformationXenotropic and Polytropic Retrovirus ReceptorInositol PhosphatesMembrane ProteinsPhosphatesPhytic AcidReceptors, G-Protein-CoupledXenotropic and Polytropic Retrovirus ReceptorXPR1 protein, human

Identifiers

PMID40128258
PMCPMC11933459

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.