Evidence map›Paper›PMID 25136126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer.

Matthew Gallon, Thomas Clairfeuille, Florian Steinberg, Caroline Mas, Rajesh Ghai, Richard B Sessions, Rohan D Teasdale, Brett M Collins, Peter J Cullen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

128 citing papers in PubMed, 188 citations in OpenAlex.

  1. Review
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  9. Endo-IP and lyso-IP toolkit for endolysosomal profiling of human-induced neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  13. Review
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  17. Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. Article

68 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 2 countries.

Matthew GallonThe Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom;
Thomas ClairfeuilleInstitute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia; and.
Florian SteinbergThe Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom;
Caroline MasInstitute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia; and.
Rajesh GhaiInstitute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia; and.
Richard B SessionsSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Rohan D TeasdaleInstitute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia; and.
Brett M CollinsInstitute for Molecular Bioscience, University of Queensland, St. Lucia, QLD 4072, Australia; and b.collins@imb.uq.edu.au pete.cullen@bristol.ac.uk.
Peter J CullenThe Henry Wellcome Integrated Signalling Laboratories, School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom; b.collins@imb.uq.edu.au pete.cullen@bristol.ac.uk.
University of Queensland · AUUniversity of Bristol · GB

Funding

Medical Research Council MR/K018299/1
6 · The paper itself

Abstract

The sorting nexin 27 (SNX27)-retromer complex is a major regulator of endosome-to-plasma membrane recycling of transmembrane cargos that contain a PSD95, Dlg1, zo-1 (PDZ)-binding motif. Here we describe the core interaction in SNX27-retromer assembly and its functional relevance for cargo sorting. Crystal structures and NMR experiments reveal that an exposed β-hairpin in the SNX27 PDZ domain engages a groove in the arrestin-like structure of the vacuolar protein sorting 26A (VPS26A) retromer subunit. The structure establishes how the SNX27 PDZ domain simultaneously binds PDZ-binding motifs and retromer-associated VPS26. Importantly, VPS26A binding increases the affinity of the SNX27 PDZ domain for PDZ- binding motifs by an order of magnitude, revealing cooperativity in cargo selection. With disruption of SNX27 and retromer function linked to synaptic dysfunction and neurodegenerative disease, our work provides the first step, to our knowledge, in the molecular description of this important sorting complex, and more broadly describes a unique interaction between a PDZ domain and an arrestin-like fold.

Indexed as

Amino Acid SequenceAnimalsArrestinBrain DiseasesCrystallography, X-RayEndocytosisEndosomesHEK293 CellsHumansMiceMolecular Sequence DataMutagenesisNerve Tissue ProteinsPDZ DomainsProtein FoldingProtein Sorting SignalsArrestinNerve Tissue ProteinsProtein Sorting SignalsRNA, Small InterferingSNX27 protein, humanSnx27 protein, mouseSnx27 protein, ratSorting NexinsVesicular Transport ProteinsVPS26A protein, humanVps26 protein, mouseAlzheimer's diseaseDown syndromeendosomal recyclingParkinson disease

Identifiers

PMID25136126
PMCPMC4156734
OpenAlexW2003443990

What Socratic holds

Textmetadata
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.