OSCR

Integrative structural analysis of human endosomal NHE6 reveals a lipid-associated gate and disordered C-terminus.

Overview

Authors: Lukas P. Feilen1, Lara K. Sach2, Emil E. Tranchant2, Milena R. Lalic2, Jesper F. Havelund3, Céline M. Jeria Cerda1, Marie Ginsthofer1, Jan Ostendorf1, Li Ma4,5, Eric M. Morrow4,5, Nils J. Færgeman3, Stine F. Pedersen2, Birthe B. Kragelund2, Henriette E. Autzen1
ORCID iDs: Lukas P. Feilen, Lara K. Sach, Milena R. Lalic, Jesper F. Havelund, Marie Ginsthofer, Eric M. Morrow, Nils J. Færgeman, Stine F. Pedersen, Birthe B. Kragelund, Henriette E. Autzen
  1. Department of Biomedical Sciences, University of Copenhagen,Copenhagen N, Denmark
  2. Department of Biology, University of Copenhagen,Copenhagen N, Denmark
  3. Department of Biochemistry and Molecular Biology, University of Southern Denmark,Odense M, Denmark
  4. Department of Molecular Biology, Cell Biology and Biochemistry, Brown University,Providence, RI USA
  5. Center for Translational Neuroscience, Carney Institute for Brain Science and Warren Alpert Medical School, Brown University,Providence, RI USA
Institutions: University of Copenhagen (Denmark); University of Southern Denmark (Denmark); Brown University (United States)
Journal: Nature communications, volume 17, issue 1, article 9663
Dates: received 18 July 2025; accepted 24 July 2026; published online 11 August 2026
Type: Research article · Language: English
License: CC BY-NC-ND
Identifiers: DOI 10.1038/s41467-026-76368-9 · PMID 42716947 · PMCID PMC13558669 · OpenAlex W7202171553
Open access: gold, a free copy (OpenAlex)
Status: data only
Categories: histology / microscopy (modality), human (organism), cellular / molecular (subfield)
Methods: Preprocessing, Evoked potentials
Keywords: Endosomes, Biophysical chemistry, Cryoelectron microscopy, Membrane proteins, Permeation and transport
MeSH: Endosomes*, Sodium-Hydrogen Exchangers*, Binding Sites, Cryoelectron Microscopy, Humans, Liposomes, Models, Molecular (* major topic)
Topic: Cellular transport and secretion (Cell Biology, Biochemistry, Genetics and Molecular Biology), according to OpenAlex
Funding: Novo Nordisk Fonden (NNF20OC0060692, NNF18OC0033926); Carlsbergfondet (Carlsberg Foundation) (CF20-0533, CF15-0425); Danmarks Frie Forskningsfond (1131-00023B); Natur og Univers, Det Frie Forskningsråd (Natural Sciences, Danish Council for Independent Research) (3103-00217B); H2020 Marie Skłodowska‐Curie Actions (101151923)
Citations: not cited yet (Europe PMC); 103 references in the paper
Research resources: RRID:Addgene_187082

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/s41467-026-76368-9.

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, 27 September 2026: the first record

Recorded: type, language, journal, volume, issue, pages, dates, 14 authors, 5 keywords, 7 MeSH terms, 5 funders, 103 references, 1 RRID.

Cite

This paper

Feilen, L. P., Sach, L. K., Tranchant, E. E., Lalic, M. R., Havelund, J. F., Jeria Cerda, C. M., Ginsthofer, M., Ostendorf, J., Ma, L., Morrow, E. M., Færgeman, N. J., Pedersen, S. F., Kragelund, B. B., & Autzen, H. E. (2026). Integrative structural analysis of human endosomal NHE6 reveals a lipid-associated gate and disordered C-terminus. Nature communications, 17(1), 9663. https://doi.org/10.1038/s41467-026-76368-9

BibTeX

@article{feilen2026integrative,
author = {Feilen, Lukas P. and Sach, Lara K. and Tranchant, Emil E. and Lalic, Milena R. and Havelund, Jesper F. and Jeria Cerda, Céline M. and Ginsthofer, Marie and Ostendorf, Jan and Ma, Li and Morrow, Eric M. and Færgeman, Nils J. and Pedersen, Stine F. and Kragelund, Birthe B. and Autzen, Henriette E.},
title = {{Integrative structural analysis of human endosomal NHE6 reveals a lipid-associated gate and disordered C-terminus}},
journal = {Nature communications},
year = {2026},
month = aug,
volume = {17},
number = {1},
pages = {9663},
publisher = {Nature Publishing Group},
issn = {2041-1723},
doi = {10.1038/s41467-026-76368-9},
url = {https://doi.org/10.1038/s41467-026-76368-9},
pmid = {42716947},
pmcid = {PMC13558669}
}

RIS

TY - JOUR
AU - Feilen, Lukas P.
AU - Sach, Lara K.
AU - Tranchant, Emil E.
AU - Lalic, Milena R.
AU - Havelund, Jesper F.
AU - Jeria Cerda, Céline M.
AU - Ginsthofer, Marie
AU - Ostendorf, Jan
AU - Ma, Li
AU - Morrow, Eric M.
AU - Færgeman, Nils J.
AU - Pedersen, Stine F.
AU - Kragelund, Birthe B.
AU - Autzen, Henriette E.
TI - Integrative structural analysis of human endosomal NHE6 reveals a lipid-associated gate and disordered C-terminus
T2 - Nature communications
J2 - Nat Commun
PY - 2026
DA - 2026/08/11
VL - 17
IS - 1
SP - 9663
SN - 2041-1723
PB - Nature Publishing Group
DO - 10.1038/s41467-026-76368-9
UR - https://doi.org/10.1038/s41467-026-76368-9
LA - en
ER -

CSL-JSON

{
"id": "10.1038/s41467-026-76368-9",
"type": "article-journal",
"title": "Integrative structural analysis of human endosomal NHE6 reveals a lipid-associated gate and disordered C-terminus",
"container-title": "Nature communications",
"author": [
{
"family": "Feilen",
"given": "Lukas P."
},
{
"family": "Sach",
"given": "Lara K."
},
{
"family": "Tranchant",
"given": "Emil E."
},
{
"family": "Lalic",
"given": "Milena R."
},
{
"family": "Havelund",
"given": "Jesper F."
},
{
"family": "Jeria Cerda",
"given": "Céline M."
},
{
"family": "Ginsthofer",
"given": "Marie"
},
{
"family": "Ostendorf",
"given": "Jan"
},
{
"family": "Ma",
"given": "Li"
},
{
"family": "Morrow",
"given": "Eric M."
},
{
"family": "Færgeman",
"given": "Nils J."
},
{
"family": "Pedersen",
"given": "Stine F."
},
{
"family": "Kragelund",
"given": "Birthe B."
},
{
"family": "Autzen",
"given": "Henriette E."
}
],
"container-title-short": "Nat Commun",
"volume": "17",
"issue": "1",
"page": "9663",
"DOI": "10.1038/s41467-026-76368-9",
"PMID": "42716947",
"PMCID": "PMC13558669",
"ISSN": "2041-1723",
"publisher": "Nature Publishing Group",
"URL": "https://doi.org/10.1038/s41467-026-76368-9",
"language": "en",
"issued": {
"date-parts": [
[
2026,
8,
11
]
]
}
}

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/s41467-026-75877-x
Structure of NHE6 and its lipid-mediated interactions regulating endosomal pH.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 24 references
[2] doi:10.1038/s41467-026-72568-5 [code]
Endosome maturation is orchestrated by inside-out proton signaling through a Na<sup>+</sup>/H<sup>+</sup> exchanger and pH-dependent Rab GTPase cycling.
Journal: Nature communications
In common: cellular / molecular, 13 references, author Eric M. Morrow
[3] doi:10.1038/s41467-026-76831-7
Structural origins of species-specific differences in TRPV2 activation.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 7 references
[4] doi:10.1038/s41467-026-74279-3
Structural basis for activation and potentiation in a human α5β3 GABA<sub>A</sub> receptor.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 6 references
[5] doi:10.1038/s41467-026-75564-x
Cooperative mechanism of neurotransmitter recognition and transport by the human vesicular polyamine transporter.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 5 references
[6] doi:10.1038/s41467-026-72780-3
Structural basis for the transport mechanism and cholesterol modulation of the human proline transporter.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 5 references
[7] doi:10.1038/s41594-026-01845-0
Conformational plasticity of human acid-sensing ion channel 1a.
Journal: Nature structural & molecular biology
In common: histology / microscopy, cellular / molecular, 5 references
[8] 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: histology / microscopy, cellular / molecular, 5 references
[9] doi:10.1038/s41467-026-75749-4 [code]
SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport.
Journal: Nature communications
In common: histology / microscopy, cellular / molecular, 4 references
[10] 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: histology / microscopy, cellular / molecular, 4 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.