Evidence map›Paper›PMID 32027819›Full record

ArticleStructure (London, England : 1993)2020

Mammalian Retromer Is an Adaptable Scaffold for Cargo Sorting from Endosomes.

Amy K Kendall, Boyang Xie, Peng Xu, Jue Wang, Rodger Burcham, Meredith N Frazier, Elad Binshtein, Hui Wei, Todd R Graham, Terunaga Nakagawa and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. VPS35 and retromer dysfunction in Parkinson's disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  9. Characterization of the First Secreted Sorting Nexin Identified in theInternational journal of molecular sciences · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Amy K KendallDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Boyang XieDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Peng XuDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA.
Jue WangCenter for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA; Department of Biochemistry, Vanderbilt University, Nashville, TN 37205, USA.
Rodger BurchamDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Meredith N FrazierDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Elad BinshteinCenter for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Hui WeiNational Resource for Automated Molecular Microscopy, New York Structural Biology Center, New York, NY 10027, USA.
Todd R GrahamDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA.
Terunaga NakagawaCenter for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA; Department of Molecular Physiology & Biophysics, Vanderbilt University, Nashville, TN 37212, USA.
Lauren P JacksonDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA; Department of Biochemistry, Vanderbilt University, Nashville, TN 37205, USA. Electronic address: lauren.p.jackson@vanderbilt.edu.
Vanderbilt University · USNew York Structural Biology Center · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
The molecular role of tepsin in membrane trafficking pathwaysR35GM119525 · NIGMS · VANDERBILT UNIVERSITY · PI Lauren Parker Jackson · 2016 to 2026
$4.3M
Mechanisms of protein transport between Golgi and endosomesR01GM118452 · NIGMS · VANDERBILT UNIVERSITY · PI GRAHAM, TODD R · 2016 to 2019
$1.4M
NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM118452NIGMS NIH HHS R35 GM119525
6 · The paper itself

Abstract

Metazoan retromer (VPS26/VPS35/VPS29) associates with sorting nexins on endosomal tubules to sort proteins to the trans-Golgi network or plasma membrane. Mechanisms of metazoan retromer assembly remain undefined. We combine single-particle cryoelectron microscopy with biophysical methods to uncover multiple oligomer structures. 2D class averages reveal mammalian heterotrimers; dimers of trimers; tetramers of trimers; and flat chains. These species are further supported by biophysical solution studies. We provide reconstructions of all species, including key sub-structures (∼5 Å resolution). Local resolution variation suggests that heterotrimers and dimers adopt multiple conformations. Our structures identify a flexible, highly conserved electrostatic dimeric interface formed by VPS35 subunits. We generate structure-based mutants to disrupt this interface in vitro. Equivalent mutations in yeast demonstrate a mild cargo-sorting defect. Our data suggest the metazoan retromer is an adaptable and plastic scaffold that accommodates interactions with different sorting nexins to sort multiple cargoes from endosomes their final destinations.

Indexed as

Protein MultimerizationAnimalsCryoelectron MicroscopyEndosomesHumansMiceMutationProtein DomainsProtein TransportSaccharomyces cerevisiaeVesicular Transport ProteinsVesicular Transport Proteinscell biologycoat proteinsmembrane traffickingsingle-particle cryo-EMstructural biology

Identifiers

PMID32027819
PMCPMC7145723
OpenAlexW3005494046

What OpenQuestion holds

Textmetadata
LicenceTDM
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.