Evidence map›Paper›PMID 36139500›Full record

ArticleCells2022

Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting.

Andrea Tirincsi, Sarah O'Keefe, Duy Nguyen, Mark Sicking, Johanna Dudek, Friedrich Förster, Martin Jung, Drazena Hadzibeganovic, Volkhard Helms, Stephen High and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Mechanisms of ER Protein Import.International journal of molecular sciences · 2022
    Article
  13. 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

12 authors at 3 institutions in 3 countries.

Andrea TirincsiMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Sarah O'KeefeSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.ORCID 0000-0002-1744-0198
Duy NguyenCenter for Bioinformatics, Saarland University, 66041 Saarbrücken, Germany.
Mark SickingMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Johanna DudekMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Friedrich FörsterBijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.ORCID 0000-0002-6044-2746
Martin JungMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.ORCID 0000-0002-1482-7020
Drazena HadzibeganovicMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Volkhard HelmsCenter for Bioinformatics, Saarland University, 66041 Saarbrücken, Germany.ORCID 0000-0002-2180-9154
Stephen HighSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.ORCID 0000-0002-4532-8152
Richard ZimmermannMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.ORCID 0000-0003-3649-1107
Sven LangMedical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.ORCID 0000-0003-1326-1851
Saarland University · DEUniversity of Manchester · GBUtrecht University · NL

Funding

Welcome Trust 204957/Z/16/Z
6 · The paper itself

Abstract

Importing proteins into the endoplasmic reticulum (ER) is essential for about 30% of the human proteome. It involves the targeting of precursor proteins to the ER and their insertion into or translocation across the ER membrane. Furthermore, it relies on signals in the precursor polypeptides and components, which read the signals and facilitate their targeting to a protein-conducting channel in the ER membrane, the Sec61 complex. Compared to the SRP- and TRC-dependent pathways, little is known about the SRP-independent/SND pathway. Our aim was to identify additional components and characterize the client spectrum of the human SND pathway. The established strategy of combining the depletion of the central hSnd2 component from HeLa cells with proteomic and differential protein abundance analysis was used. The SRP and TRC targeting pathways were analyzed in comparison. TMEM109 was characterized as hSnd3. Unlike SRP but similar to TRC, the SND clients are predominantly membrane proteins with N-terminal, central, or C-terminal targeting signals.

Indexed as

ProteomicsSignal Recognition ParticleEndoplasmic ReticulumHeLa CellsHumansMembrane ProteinsPeptidesProteomeSEC Translocation ChannelsMembrane ProteinsPeptidesProteomeSEC Translocation ChannelsSignal Recognition Particledifferential protein abundance analysisendoplasmic reticulumguided entry of tail-anchored proteinsmembrane proteinsprotein targetingprotein translocationSec61 complexsignal recognition particleSRP-independent targeting

Identifiers

PMID36139500
PMCPMC9496750
OpenAlexW4296526972

What OpenQuestion holds

Textmetadata
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.