Evidence map›Paper›PMID 22505607›Full record

ArticleJournal of cell science2012

TRC40 can deliver short secretory proteins to the Sec61 translocon.

Nicholas Johnson, Fabio Vilardi, Sven Lang, Pawel Leznicki, Richard Zimmermann, Stephen High

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Hepatitis C Virus Structure: Defined by What It Is Not.Cold Spring Harbor perspectives in medicine · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Nicholas JohnsonFaculty of Life Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.
Fabio Vilardi
Sven Lang
Pawel Leznicki
Richard Zimmermann
Stephen High
University of Manchester · GBSaarland University · DEHeidelberg University · DE

Funding

Biotechnology and Biological Sciences Research Council BB/D005752/1Wellcome Trust WT092107
6 · The paper itself

Abstract

Whilst the co-translational translocation of nascent proteins across the mammalian endoplasmic reticulum (ER) is well defined, the capacity of this organelle for post-translational translocation is poorly delineated. Here we identify two human secretory protein precursors, apelin and statherin, as bona fide substrates for post-translational translocation across the ER membrane. Further studies, in combination with Hyalophora cecropia preprocecropin A (ppcecA), show that all three proteins bind to TRC40 and can utilise this component for their delivery to the ER membrane in a well-established in vitro system. However, ppcecA is not an obligate TRC40 substrate, and it can also be delivered to the ER by an alternative TRC40-independent pathway. Upon arrival at the ER membrane, these short secretory proteins appear to be ubiquitously transported across the ER membrane through the Sec61 translocon, apparently irrespective of their delivery route. We speculate that the post-translational translocation of secretory proteins in higher eukaryotes is more prevalent than previously acknowledged.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsApelinArsenite Transporting ATPasesDogsEndoplasmic ReticulumHSC70 Heat-Shock ProteinsHumansHydrazonesHydroxyureaIntercellular Signaling Peptides and ProteinsIntracellular MembranesMembrane ProteinsMembrane Transport ProteinsMolecular Sequence Data1-(4-chlorophenyl)-3-(3-(4-chlorophenyl)-5,5-dimethyl-1-(3-(5-nitrofuran-2-yl)allyldienehydrazinocarbonylmethyl)-2-oxoimidazolidin-4-yl)-1-hydroxyureaApelinAPLN protein, humanArsenite Transporting ATPasesGET1 protein, humanGET3 protein, humanHSC70 Heat-Shock ProteinsHSPA8 protein, humanHydrazonesHydroxyureaIntercellular Signaling Peptides and ProteinsMembrane ProteinsMembrane Transport ProteinsNuclear ProteinsSalivary Proteins and PeptidesSEC Translocation ChannelsSTATH protein, human

Identifiers

PMID22505607
PMCPMC3445324
OpenAlexW2117023179

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.