Evidence map›Paper›PMID 31337624›Full record

ArticleThe Journal of cell biology2019

A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling.

Sho W Suzuki, Ya-Shan Chuang, Ming Li, Matthew N J Seaman, Scott D Emr

Abstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
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  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Navigating the Controversies of Retromer-Mediated Endosomal Protein Sorting.Frontiers in cell and developmental biology · 2021
    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

5 authors.

Sho W Suzuki *Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY.
Ya-Shan Chuang *Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY.
Ming LiWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY.ORCID 0000-0002-1247-2377
Matthew N J SeamanUniversity of Cambridge, Cambridge Institute for Medical Research, Addenbrookes Hospital, Cambridge, UK.ORCID 0000-0001-9916-3245
Scott D EmrWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY sde26@cornell.edu.ORCID 0000-0002-5408-6781

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as ØX[L/M/V], where Ø is F/Y/W. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How then does retromer precisely select its cargos? Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, retromer interacts with cargos in a more complex manner than previously thought, which facilitates precise cargo recognition.

Indexed as

Binding SitesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsPEP8 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS35 protein, S cerevisiae

Identifiers

PMID31337624
PMCPMC6719449

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Registered trials

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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.