Evidence map›Paper›PMID 42581050›Full record

ArticleNature communications2026

Structure of NHE6 and its lipid-mediated interactions regulating endosomal pH.

Sukkyeong Jung, Hyunku Yeo, Hang Li, Surabhi Kokane, Tom Reichenbach, Ashutosh Gulati, Giuseppe Albano, Carla Kirschbaum, Tin Manh Ho, Michael Landreh and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

14 authors.

Sukkyeong Jung *Department of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-4730-5245
Hyunku Yeo *Department of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-8701-8902
Hang Li *Department of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.
Surabhi KokaneDepartment of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.
Tom ReichenbachDepartment of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.
Ashutosh GulatiDepartment of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden.ORCID 0000-0003-0960-994X
Giuseppe AlbanoDepartment of Nephrology and Hypertension, Inselspital, Bern University Hospital and University of Bern, Bern, Switzerland.
Carla KirschbaumDepartment of Chemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford, Oxford, UK.ORCID 0000-0003-3192-0785
Tin Manh HoDepartment of Nephrology and Hypertension, Inselspital, Bern University Hospital and University of Bern, Bern, Switzerland.ORCID 0000-0003-1608-2234
Michael LandrehDepartment of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-7958-4074
Mia AbramssonDepartment of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-8184-0145
Carol V RobinsonDepartment of Chemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford, Oxford, UK.ORCID 0000-0001-7829-5505
Daniel G FusterDepartment of Nephrology and Hypertension, Inselspital, Bern University Hospital and University of Bern, Bern, Switzerland.
David DrewDepartment of Biochemistry and Biophysics, Science for Life laboratory, Stockholm University, Stockholm, Sweden. ddrew@dbb.su.se.ORCID 0000-0001-8866-6349

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sodium-proton exchangers (NHEs) are found in all cells to regulate intracellular pH, sodium levels and cell volume. In humans, there are nine different NHE transporters (SLC9A1-9), which vary in tissue distribution, kinetics and regulation. NHE6 localizes to endosomal membranes and mutations in the protein are known to cause the X-linked neurological disorder Christianson syndrome. Despite its importance, the structural basis of NHE6 function and regulation is unclear. Here we report four cryo-electron microscopy structures of rat NHE6 between 2.2 and 3.3 Å resolution, revealing its homodimeric structure, ion binding and remodelling by lipids. We characterize a lipid-binding site between the protomers that accommodates the endosomal-specific phosphatidylinositol 3-phosphate (PI3P) lipid. Using solid-supported membrane (SSM)-based electrophysiology we demonstrate that NHE6 transports both Na

Indexed as

EndosomesSodium-Hydrogen ExchangersAnimalsBinding SitesCryoelectron MicroscopyHumansHydrogen-Ion ConcentrationPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPotassiumProtein BindingRatsSodiumphosphatidylinositol 3-phosphatePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPotassiumSodiumSodium-Hydrogen Exchangers

Identifiers

PMID42581050
PMCPMC13463026

What OpenQuestion holds

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Registered trials

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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 OpenQuestion graph.