Evidence map›Paper›PMID 27889239›Full record

ArticleCell2016

Structural Mechanism for Cargo Recognition by the Retromer Complex.

María Lucas, David C Gershlick, Ander Vidaurrazaga, Adriana L Rojas, Juan S Bonifacino, Aitor Hierro

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers.

0numbers the graph read from it
0cells of the map it votes in
146citing papers in PubMed
12.7field-weighted citation impact, top 1% 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

146 citing papers in PubMed, 220 citations in OpenAlex.

  1. SNX3 exacerbates hepatic fibrosis by amplifying TGF-Acta pharmaceutica Sinica. B · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Cargo-Adaptor Cooperation Programs Retromer Coat Architecture.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. The Rab5 effector Rabankyrin-5 mediates endosomal fusion and trafficking of human papillomavirus during early entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. SNX-3 confers lysosomal fusion-competence to sustain basal autophagy.Cellular and molecular life sciences : CMLS · 2026
    Article
  13. Article
  14. Sorting nexin 3 promotes ischemic retinopathy through RIP1- and RIP3-mediated myeloid cell necroptosis and mitochondrial fission.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

María LucasStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain.
David C GershlickCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Ander VidaurrazagaStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain.
Adriana L RojasStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain.
Juan S BonifacinoCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: bonifacinoj@helix.nih.gov.
Aitor HierroStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain; IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Spain. Electronic address: ahierro@cicbiogune.es.
CIC bioGUNE · ESNational Institutes of Health · USIkerbasque · ES

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
REGULATION OF THE FATE OF NEWLY SYNTHESIZED PROTEINSZ01HD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 1991 to 2008
$4.4M
Intramural NIH HHS Z01 HD001607Intramural NIH HHS ZIA HD001607
6 · The paper itself

Abstract

Retromer is a multi-protein complex that recycles transmembrane cargo from endosomes to the trans-Golgi network and the plasma membrane. Defects in retromer impair various cellular processes and underlie some forms of Alzheimer's disease and Parkinson's disease. Although retromer was discovered over 15 years ago, the mechanisms for cargo recognition and recruitment to endosomes have remained elusive. Here, we present an X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II. This analysis identifies a binding site for canonical recycling signals at the interface between VPS26 and SNX3. In addition, the structure highlights a network of cooperative interactions among the VPS subunits, SNX3, and cargo that couple signal-recognition to membrane recruitment.

Indexed as

Amino Acid SequenceCation Transport ProteinsCrystallography, X-RayHumansModels, MolecularMultiprotein ComplexesProtein IsoformsScattering, Small AngleSolute Carrier Family 11, Member 2Sorting NexinsVesicular Transport ProteinsCation Transport ProteinsMultiprotein ComplexesProtein IsoformsSNX3 protein, humanSolute Carrier Family 11, Member 2Sorting NexinsVesicular Transport ProteinsVPS26A protein, humanVPS35 protein, humancargo recognitionendocytic recyclingendosomesmembrane recruitmentmembrane tubulesprotein coatsretrograde transportretromersorting nexinssorting signals

Identifiers

PMID27889239
PMCPMC5147500
OpenAlexW2553944165

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.