OSCR

Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter.

Overview

Authors: Yue Zhou1, Ningqin Wang2, Jiaqi Wang2, Xinrui Meng1, Jing-Xiang Wu1
  1. State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China
  2. School of Life Sciences and Biopharmaceutics, Shenyang Pharmaceutical University, Shenyang, China
Journal: Nature communications, volume 17, issue 1, article 7285
Dates: received 17 October 2025; accepted 21 April 2026; published online 6 May 2026
Type: Research article · Language: English
License: CC BY-NC-ND
Identifiers: DOI 10.1038/s41467-026-72780-3 · PMID 42091899 · PMCID PMC13402342 · OpenAlex W7160438125
Open access: gold, a free copy (OpenAlex)
Status: data only
Categories: histology / microscopy (modality), human (organism), cellular / molecular (subfield)
Methods: Statistics, Evoked potentials, fMRI & imaging
Keywords: Cryoelectron microscopy, Transporters in the nervous system, Neurochemistry, Permeation and transport
MeSH: Amino Acid Transport Systems, Neutral*, Cholesterol*, Proline*, Binding Sites, Biological Transport, Cryoelectron Microscopy, Humans, Kinetics, Models, Molecular, Protein Conformation (* major topic)
Topic: Amino Acid Enzymes and Metabolism (Biochemistry, Biochemistry, Genetics and Molecular Biology), according to OpenAlex
Funding: National Natural Science Foundation of China (National Science Foundation of China) (32522046, 32371266)
Citations: not cited yet (Europe PMC); 57 references in the paper

Abstract

The abstract is not reproduced here: the paper's license (CC BY-NC-ND) does not allow it. Read it in the paper, at the publisher or on Europe PMC.

Code

The paper links to its data, not to its authors' code: see the Data section.

The paper's code and data availability statement is in the Data section.

Tracing map

A tracing map links a paper to the code its authors published: this paper has none, so it has no map.

Data

Datasets cited

Code and data availability statement

The paper has a code and data availability statement. Its license (CC BY-NC-ND) does not allow reproducing it here; in short, from what the harvester recognized in it:

Read it in the paper: doi.org/10.1038/s41467-026-72780-3.

Versions

The history of this record: each version stored by the harvester or made by a correction of its authors or of the maintainers of its code, and what changed in its facts. The texts of the paper (its abstract, its availability statements) are not part of it; versions that changed only those are not listed.

Version 1, 28 September 2026: the first record

Recorded: type, language, journal, volume, issue, pages, dates, 5 authors, 4 keywords, 10 MeSH terms, 1 funder, 57 references.

Cite

This paper

Zhou, Y., Wang, N., Wang, J., Meng, X., & Wu, J.-X. (2026). Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter. Nature communications, 17(1), 7285. https://doi.org/10.1038/s41467-026-72780-3

BibTeX

@article{zhou2026structural,
author = {Zhou, Yue and Wang, Ningqin and Wang, Jiaqi and Meng, Xinrui and Wu, Jing-Xiang},
title = {{Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter}},
journal = {Nature communications},
year = {2026},
month = may,
volume = {17},
number = {1},
pages = {7285},
publisher = {Nature Publishing Group},
issn = {2041-1723},
doi = {10.1038/s41467-026-72780-3},
url = {https://doi.org/10.1038/s41467-026-72780-3},
pmid = {42091899},
pmcid = {PMC13402342}
}

RIS

TY - JOUR
AU - Zhou, Yue
AU - Wang, Ningqin
AU - Wang, Jiaqi
AU - Meng, Xinrui
AU - Wu, Jing-Xiang
TI - Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter
T2 - Nature communications
J2 - Nat Commun
PY - 2026
DA - 2026/05/06
VL - 17
IS - 1
SP - 7285
SN - 2041-1723
PB - Nature Publishing Group
DO - 10.1038/s41467-026-72780-3
UR - https://doi.org/10.1038/s41467-026-72780-3
LA - en
ER -

CSL-JSON

{
"id": "10.1038/s41467-026-72780-3",
"type": "article-journal",
"title": "Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter",
"container-title": "Nature communications",
"author": [
{
"family": "Zhou",
"given": "Yue"
},
{
"family": "Wang",
"given": "Ningqin"
},
{
"family": "Wang",
"given": "Jiaqi"
},
{
"family": "Meng",
"given": "Xinrui"
},
{
"family": "Wu",
"given": "Jing-Xiang"
}
],
"container-title-short": "Nat Commun",
"volume": "17",
"issue": "1",
"page": "7285",
"DOI": "10.1038/s41467-026-72780-3",
"PMID": "42091899",
"PMCID": "PMC13402342",
"ISSN": "2041-1723",
"publisher": "Nature Publishing Group",
"URL": "https://doi.org/10.1038/s41467-026-72780-3",
"language": "en",
"issued": {
"date-parts": [
[
2026,
5,
6
]
]
}
}

Similar papers

The papers with a page that share the most with this one: the tools found in their code, their categories, datasets, cited references and authors, the rarest counting most.

[1] doi:10.1038/s41467-026-71935-6
Transport and inhibition mechanisms of human glycine transporter 2.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 12 references, author Jing-Xiang Wu
[2] doi:10.1038/s41467-026-76831-7
Structural origins of species-specific differences in TRPV2 activation.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 6 references
[3] doi:10.1038/s41467-026-70575-0
Structure of a pH-sensitive pentameric ligand-gated ion channel from the Sarcoptes scabies mite.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 5 references
[4] doi:10.1038/s41467-026-74814-2
Structural mechanism of Necrocide 1 activation of human TRPM4 that triggers necrosis by sodium overload.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 4 references
[5] doi:10.1038/s41594-026-01845-0
Conformational plasticity of human acid-sensing ion channel 1a.
Journal: Nature structural & molecular biology
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 4 references
[6] doi:10.1038/s41467-026-70190-z [code]
Structural insights into insect-selective sodium channel toxins drive AI-enhanced biopesticide design.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 4 references
[7] doi:10.1038/s41467-026-75877-x
Structure of NHE6 and its lipid-mediated interactions regulating endosomal pH.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 4 references
[8] doi:10.1038/s41467-026-75444-4 [code]
Structural insights enable drug discovery for the neuronal NBCn2 carbonate transporter.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 4 references
[9] doi:10.1038/s41467-026-75941-6
Structural and functional studies of inward rectifier Kir7.1 and its regulation by the Melanocortin-4 receptor.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 3 references
[10] doi:10.1038/s41467-026-75806-y [code]
Cryo-EM insights into isoform-specific properties of the IP<sub>3</sub>R2 channel.
Journal: Nature communications
In common: ebi.ac.uk/pdbe/entry, histology / microscopy, cellular / molecular, 3 references

Contribute

The authors of this paper can claim it, correct its record and validate its tracing map, and the maintainers of its code (its owner, or a public member of its organization) correct what it says of their repository; anyone signed in can ask for its removal. Every request goes to OSCR's own machine, which answers it; your account page follows them.

Sign in with ORCID to claim this paper as one of its authors, correct its record or validate its tracing map: when the paper's metadata lists your ORCID iD, you are recognized at once. Maintainers of its code: sign in with GitHub, then claim the repository on your account page.

Request its removal

To ask OSCR to remove this record, the copies of its authors' scripts or its tracing map, use the removal request page: signed in, you say who you are, what to remove and why, then review and confirm the request. Published rules decide every request (how).

Discussion, reproductions, activity

Discussion: questions and error reports about this paper and its code, from signed-in readers and its authors. It opens with sign-in.

Reproductions: reports from readers who ran the authors' code: what they reproduced, with which environment, commit and data. It opens with sign-in.

Activity: what happens around this paper: new versions of its record, its map's validation, discussions and reproductions. It opens with sign-in.