Evidence map›Paper›PMID 24519942›Full record

ArticleThe Journal of biological chemistry2014

Protein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains.

Martin Loibl, Lina Wunderle, Johannes Hutzler, Benjamin L Schulz, Markus Aebi, Sabine Strahl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.Molecular & cellular proteomics : MCP · 2016
    Article
  12. Article
  13. ERAD and how viruses exploit it.Frontiers in microbiology · 2014
    Review
  14. Article
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

6 authors at 2 institutions in 2 countries.

Martin LoiblFrom the Centre for Organismal Studies (COS), Cell Chemistry, Heidelberg University, 69120 Heidelberg, Germany and.
Lina Wunderle
Johannes Hutzler
Benjamin L Schulz
Markus Aebi
Sabine Strahl
Heidelberg University · DEBoard of the Swiss Federal Institutes of Technology · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-Mannosylation and N-glycosylation are essential protein modifications that are initiated in the endoplasmic reticulum (ER). Protein translocation across the ER membrane and N-glycosylation are highly coordinated processes that take place at the translocon-oligosaccharyltransferase (OST) complex. In analogy, it was assumed that protein O-mannosyltransferases (PMTs) also act at the translocon, however, in recent years it turned out that prolonged ER residence allows O-mannosylation of un-/misfolded proteins or slow folding intermediates by Pmt1-Pmt2 complexes. Here, we reinvestigate protein O-mannosylation in the context of protein translocation. We demonstrate the association of Pmt1-Pmt2 with the OST, the trimeric Sec61, and the tetrameric Sec63 complex in vivo by co-immunoprecipitation. The coordinated interplay between PMTs and OST in vivo is further shown by a comprehensive mass spectrometry-based analysis of N-glycosylation site occupancy in pmtΔ mutants. In addition, we established a microsomal translation/translocation/O-mannosylation system. Using the serine/threonine-rich cell wall protein Ccw5 as a model, we show that PMTs efficiently mannosylate proteins during their translocation into microsomes. This in vitro system will help to unravel mechanistic differences between co- and post-translocational O-mannosylation.

Indexed as

GlycosylationMannosyltransferasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMannosyltransferasesprotein O-mannosyltransferaseSaccharomyces cerevisiae ProteinsEndoplasmic Reticulum (ER)GlycosylationGlycosyltransferasesO-MannosylationOSTPMTProtein TranslocationYeast

Identifiers

PMID24519942
PMCPMC3961683
OpenAlexW1969434770

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.