Evidence map›Paper›PMID 31541095›Full record

ArticleNature communications2019

Regulation of the endosomal SNX27-retromer by OTULIN.

Aurelia Stangl, Paul R Elliott, Adan Pinto-Fernandez, Sarah Bonham, Luke Harrison, Annalisa Schaub, Kerstin Kutzner, Kirstin Keusekotten, Paul T Pfluger, Farid El Oualid and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.7field-weighted citation impact, top 5% of its field
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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Variation inCirculation research · 2026
    Article
  3. Article
  4. Linear ubiquitination of the NMDA receptor GluN2A subunit facilitates the GluN2B-to-GluN2A switch and synaptic maturation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  7. Article
  8. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
  9. Review
  10. FishJournal of virology · 2024
    Article
  11. Review
  12. Dominant negative OTULIN-related autoinflammatory syndrome.The Journal of experimental medicine · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Deubiquitinases in cancer.Nature reviews. Cancer · 2023
    Review
  18. Article
  19. Article
  20. 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

13 authors at 3 institutions in 3 countries.

Aurelia StanglResearch Unit Cellular Signal Integration, Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München, Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany.
Paul R ElliottMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. paul.elliott@bioch.ox.ac.uk.
Adan Pinto-FernandezTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, UK.
Sarah BonhamTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, UK.
Luke HarrisonResearch Unit Neurobiology of Diabetes, Institute for Diabetes and Obesity, Helmholtz Zentrum München, German Centre for Diabetes Research (DZD), Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany.
Annalisa SchaubResearch Unit Cellular Signal Integration, Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München, Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany.
Kerstin KutznerResearch Unit Cellular Signal Integration, Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München, Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany.
Kirstin KeusekottenMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Paul T PflugerResearch Unit Neurobiology of Diabetes, Institute for Diabetes and Obesity, Helmholtz Zentrum München, German Centre for Diabetes Research (DZD), Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany.ORCID http://orcid.org/0000-0002-8118-7588
Farid El OualidUbiQ Bio BV, Science Park 408, 1098 XH, Amsterdam, The Netherlands.ORCID http://orcid.org/0000-0002-4447-9960
Benedikt M KesslerTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, UK.ORCID http://orcid.org/0000-0002-8160-2446
David KomanderMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. dk@wehi.edu.au.
Daniel KrappmannResearch Unit Cellular Signal Integration, Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München, Ingolstaedter Landstrasse 1, 85764, Neuherberg, Germany. daniel.krappmann@helmholtz-muenchen.de.ORCID http://orcid.org/0000-0001-7640-3234
Helmholtz Zentrum München · DEMRC Laboratory of Molecular Biology · GBUniversity of Oxford · GB

Funding

Medical Research Council MC_U105192732Medical Research Council MR/R008582/1
6 · The paper itself

Abstract

OTULIN (OTU Deubiquitinase With Linear Linkage Specificity) specifically hydrolyzes methionine1 (Met1)-linked ubiquitin chains conjugated by LUBAC (linear ubiquitin chain assembly complex). Here we report on the mass spectrometric identification of the OTULIN interactor SNX27 (sorting nexin 27), an adaptor of the endosomal retromer complex responsible for protein recycling to the cell surface. The C-terminal PDZ-binding motif (PDZbm) in OTULIN associates with the cargo-binding site in the PDZ domain of SNX27. By solving the structure of the OTU domain in complex with the PDZ domain, we demonstrate that a second interface contributes to the selective, high affinity interaction of OTULIN and SNX27. SNX27 does not affect OTULIN catalytic activity, OTULIN-LUBAC binding or Met1-linked ubiquitin chain homeostasis. However, via association, OTULIN antagonizes SNX27-dependent cargo loading, binding of SNX27 to the VPS26A-retromer subunit and endosome-to-plasma membrane trafficking. Thus, we define an additional, non-catalytic function of OTULIN in the regulation of SNX27-retromer assembly and recycling to the cell surface.

Indexed as

Binding SitesCrystallography, X-RayEndopeptidasesEndosomesGene Knockout TechniquesGlucose Transporter Type 1HEK293 CellsHumansModels, MolecularPDZ DomainsProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein TransportSorting NexinsUbiquitinationEndopeptidasesGlucose Transporter Type 1OTULIN protein, humanSLC2A1 protein, humanSNX27 protein, humanSorting NexinsVesicular Transport ProteinsVPS26A protein, human

Identifiers

PMID31541095
PMCPMC6754446
OpenAlexW2973966495

What Socratic holds

Textmetadata
LicenceCC BY
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.