Evidence map›Paper›PMID 30217974›Full record

ArticleNature communications2018

Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import.

Duy Nguyen, Regine Stutz, Stefan Schorr, Sven Lang, Stefan Pfeffer, Hudson H Freeze, Friedrich Förster, Volkhard Helms, Johanna Dudek, Richard Zimmermann

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 99 citations in OpenAlex.

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  8. Review
  9. Review
  10. Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025
    Article
  11. TheeLife · 2025
    Article
  12. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  13. Review
  14. Article
  15. Article
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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

10 authors at 4 institutions in 3 countries.

Duy NguyenCenter for Bioinformatics, Saarland University, 66041, Saarbrücken, Germany.
Regine StutzMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Stefan SchorrMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Sven LangMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Stefan PfefferMax-Planck Institute of Biochemistry, Department of Molecular Structural Biology, 82152, Martinsried, Germany.
Hudson H FreezeSanford-Burnham-Prebys Medical Discovery Institute, La Jolla, CA, 92037, USA.
Friedrich FörsterBijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.
Volkhard HelmsCenter for Bioinformatics, Saarland University, 66041, Saarbrücken, Germany. volkhard.helms@bioinformatik.uni-saarland.de.ORCID http://orcid.org/0000-0002-2180-9154
Johanna DudekMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany. johanna.dudek@uks.eu.
Richard ZimmermannMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany. richard.zimmermann@uks.eu.
Saarland University · DEMax Planck Institute of Biochemistry · DESanford Burnham Prebys Medical Discovery Institute · USUtrecht University · NL

Funding

New Congenital Disorders of Glycosylation: Therapy and ModelsR01DK099551 · NIDDK · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Hudson H. Freeze · 2014 to 2026
$6.7M
Deutsche Forschungsgemeinschaft (German Research Foundation) FO716/4-1Deutsche Forschungsgemeinschaft (German Research Foundation) IRTG1830Deutsche Forschungsgemeinschaft (German Research Foundation) ZI234/13-1NIDDK NIH HHS R01 DK099551
6 · The paper itself

Abstract

In mammalian cells, one-third of all polypeptides are transported into or across the ER membrane via the Sec61 channel. While the Sec61 complex facilitates translocation of all polypeptides with amino-terminal signal peptides (SP) or transmembrane helices, the Sec61-auxiliary translocon-associated protein (TRAP) complex supports translocation of only a subset of precursors. To characterize determinants of TRAP substrate specificity, we here systematically identify TRAP-dependent precursors by analyzing cellular protein abundance changes upon TRAP depletion using quantitative label-free proteomics. The results are validated in independent experiments by western blotting, quantitative RT-PCR, and complementation analysis. The SPs of TRAP clients exhibit above-average glycine-plus-proline content and below-average hydrophobicity as distinguishing features. Thus, TRAP may act as SP receptor on the ER membrane's cytosolic face, recognizing precursor polypeptides with SPs of high glycine-plus-proline content and/or low hydrophobicity, and triggering substrate-specific opening of the Sec61 channel through interactions with the ER-lumenal hinge of Sec61α.

Indexed as

Protein Sorting SignalsProtein TransportBlotting, WesternCalcium-Binding ProteinsEndoplasmic ReticulumGlycineHeLa CellsHumansHydrophobic and Hydrophilic InteractionsMembrane GlycoproteinsProlineProteomicsReal-Time Polymerase Chain ReactionReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation ChannelsCalcium-Binding ProteinsGlycineMembrane GlycoproteinsProlineProtein Sorting SignalsReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC61A1 protein, humanSEC Translocation Channelssignal sequence receptor

Identifiers

PMID30217974
PMCPMC6138672
OpenAlexW2890986735

What OpenQuestion holds

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LicenceCC BY
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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.