Evidence map›Paper›PMID 32651229›Full record

ArticleThe Journal of biological chemistry2020

Retromer forms low order oligomers on supported lipid bilayers.

Catherine L Deatherage, Joerg Nikolaus, Erdem Karatekin, Christopher G Burd

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  8. Review
  9. Article
  10. Navigating the Controversies of Retromer-Mediated Endosomal Protein Sorting.Frontiers in cell and developmental biology · 2021
    Review
  11. Article
  12. Article
  13. Unveiling the cryo-EM structure of retromer.Biochemical Society transactions · 2020
    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

4 authors at 2 institutions in 2 countries.

Catherine L DeatherageDepartment of Cell Biology, Yale School of Medicine, New Haven, Connecticut, USA.
Joerg NikolausDepartment of Cellular and Molecular Physiology, Yale School of Medicine, New Haven, Connecticut, USA.
Erdem KaratekinDepartment of Cellular and Molecular Physiology, Yale School of Medicine, New Haven, Connecticut, USA; Nanobiology Institute, Yale University, West Haven, Connecticut, USA; Department of Molecular Biophysics and Biochemistry, Yale School of Medicine, New Haven, Connecticut, USA; Saints-Pères Paris Institute for the Neurosciences (SPPIN), CNRS, Université de Paris, Paris, France. Electronic address: erdem.karatekin@yale.edu.
Christopher G BurdDepartment of Cell Biology, Yale School of Medicine, New Haven, Connecticut, USA. Electronic address: christopher.burd@yale.edu.
Yale University · USCentre National de la Recherche Scientifique · FR

Funding

Sorting and Trafficking in the Endosomal SystemR37GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2017 to 2021
$2.0M
Nucleation and dynamics of exocytotic fusion poresR01NS113236 · NINDS · YALE UNIVERSITY · PI KARATEKIN, ERDEM · 2019 to 2023
$1.8M
Reconstitution of retromer dependent cargo sortingF32GM125120 · NIGMS · YALE UNIVERSITY · PI DEATHERAGE, CATHERINE L · 2018 to 2019
$123k
NIGMS NIH HHS F32 GM125120NIGMS NIH HHS R37 GM061221NINDS NIH HHS R01 NS113236
6 · The paper itself

Abstract

Retromer orchestrates the selection and export of integral membrane proteins from the endosome via retrograde and plasma membrane recycling pathways. Long-standing hypotheses regarding the retromer sorting mechanism posit that oligomeric interactions between retromer and associated accessory factors on the endosome membrane drives clustering of retromer-bound integral membrane cargo prior to its packaging into a nascent transport carrier. To test this idea, we examined interactions between components of the sorting nexin 3 (SNX3)-retromer sorting pathway using quantitative single particle fluorescence microscopy in a reconstituted system. This system includes a supported lipid bilayer, fluorescently labeled retromer, SNX3, and two model cargo proteins, RAB7, and retromer-binding segments of the WASHC2C subunit of the WASH complex. We found that the distribution of membrane-associated retromer is predominantly comprised of monomer (∼18%), dimer (∼35%), trimer (∼24%), and tetramer (∼13%). Unexpectedly, neither the presence of membrane-associated cargo nor accessory factors substantially affected this distribution. The results indicate that retromer has an intrinsic propensity to form low order oligomers on a supported lipid bilayer and that neither membrane association nor accessory factors potentiate oligomerization. The results support a model whereby SNX3-retromer is a minimally concentrative coat protein complex adapted to bulk membrane trafficking from the endosomal system.

Indexed as

HumansLipid BilayersMultiprotein ComplexesPhosphate-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSorting NexinsLipid BilayersMultiprotein ComplexesPhosphate-Binding Proteinsrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab GTP-Binding ProteinsSNX3 protein, humanSorting NexinsWASHC2C protein, humanbiochemical reconstitutioncell biologymembrane bilayeroligomerizationretromersingle particle analysistraffickingWASHC2C

Identifiers

PMID32651229
PMCPMC7443500
OpenAlexW3042073900

What OpenQuestion 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 OpenQuestion graph.