Evidence map›Paper›PMID 27528657›Full record

ArticleThe Journal of cell biology2016

Atypical parkinsonism-associated retromer mutant alters endosomal sorting of specific cargo proteins.

Kirsty J McMillan, Matthew Gallon, Adam P Jellett, Thomas Clairfeuille, Frances C Tilley, Ian McGough, Chris M Danson, Kate J Heesom, Kevin A Wilkinson, Brett M Collins and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 56 citations in OpenAlex.

  1. VPS29C: Adding complexity to the Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Unveiling the cryo-EM structure of retromer.Biochemical Society transactions · 2020
    Review
  15. Article
  16. Review
  17. Coatopathies: Genetic Disorders of Protein Coats.Annual review of cell and developmental biology · 2019
    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

11 authors at 2 institutions in 2 countries.

Kirsty J McMillanSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Matthew GallonSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Adam P JellettSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Thomas ClairfeuilleInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland 4072, Australia.
Frances C TilleySchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Ian McGoughSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.ORCID 0000-0002-4622-5358
Chris M DansonSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Kate J HeesomProteomics Facility, School of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.ORCID 0000-0002-5418-5392
Kevin A WilkinsonSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK.
Brett M CollinsInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland 4072, Australia.
Peter J CullenSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, England, UK pete.cullen@bristol.ac.uk.
University of Bristol · GBThe University of Queensland · AU

Funding

Medical Research Council MR/K018299/1Medical Research Council MR/K501359/1Wellcome Trust 083474Wellcome Trust 089928Wellcome Trust 104568
6 · The paper itself

Abstract

The retromer complex acts as a scaffold for endosomal protein complexes that sort integral membrane proteins to various cellular destinations. The retromer complex is a heterotrimer of VPS29, VPS35, and VPS26. Two of these paralogues, VPS26A and VPS26B, are expressed in humans. Retromer dysfunction is associated with neurodegenerative disease, and recently, three VPS26A mutations (p.K93E, p.M112V, and p.K297X) were discovered to be associated with atypical parkinsonism. Here, we apply quantitative proteomics to provide a detailed description of the retromer interactome. By establishing a comparative proteomic methodology, we identify how this interactome is perturbed in atypical parkinsonism-associated VPS26A mutants. In particular, we describe a selective defect in the association of VPS26A (p.K297X) with the SNX27 cargo adaptor. By showing how a retromer mutant leads to altered endosomal sorting of specific PDZ ligand-containing cargo proteins, we reveal a new mechanism for perturbed endosomal cargo sorting in atypical parkinsonism.

Indexed as

Cell LineEndosomesHumansMutationParkinsonian DisordersProtein Interaction MappingProtein SubunitsProtein TransportSorting NexinsProtein SubunitsSNX27 protein, humanSorting Nexins

Identifiers

PMID27528657
PMCPMC4987296
OpenAlexW2510207246

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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 OpenQuestion graph.