Evidence map›Paper›PMID 16822836›Full record

ArticleMolecular biology of the cell2006

The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability.

Tina Junne, Torsten Schwede, Veit Goder, Martin Spiess

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Functional asymmetry within the Sec61p translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. The bacterial translocon SecYEG opens upon ribosome binding.The Journal of biological chemistry · 2013
    Article
  15. Protein translocation across the rough endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013
    Review
  16. Article
  17. Article
  18. Direct simulation of early-stage Sec-facilitated protein translocation.Journal of the American Chemical Society · 2012
    Article
  19. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  20. 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

4 authors.

Tina JunneBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
Torsten Schwede
Veit Goder
Martin Spiess

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Sec61/SecY translocon mediates translocation of proteins across the membrane and integration of membrane proteins into the lipid bilayer. The structure of the translocon revealed a plug domain blocking the pore on the lumenal side. It was proposed to be important for gating the protein conducting channel and for maintaining the permeability barrier in its unoccupied state. Here, we analyzed in yeast the effect of introducing destabilizing point mutations in the plug domain or of its partial or complete deletion. Unexpectedly, even when the entire plug domain was deleted, cells were viable without growth phenotype. They showed an effect on signal sequence orientation of diagnostic signal-anchor proteins, a minor defect in cotranslational and a significant deficiency in posttranslational translocation. Steady-state levels of the mutant protein were reduced, and when coexpressed with wild-type Sec61p, the mutant lacking the plug competed poorly for complex partners. The results suggest that the plug is unlikely to be important for sealing the translocation pore in yeast but that it plays a role in stabilizing Sec61p during translocon formation.

Indexed as

Cell SurvivalMembrane ProteinsMembrane Transport ProteinsProtein Sorting SignalsProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsSequence DeletionMembrane ProteinsMembrane Transport ProteinsProtein Sorting SignalsSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation Channels

Identifiers

PMID16822836
PMCPMC1556385

What OpenQuestion holds

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Read underepoch 390

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.