Evidence map›Paper›PMID 17242069›Full record

ArticleThe Journal of cell biology2007

SecY alterations that impair membrane protein folding and generate a membrane stress.

Nobuyuki Shimohata, Shushi Nagamori, Yoshinori Akiyama, H Ronald Kaback, Koreaki Ito

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-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

25 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. The divergentMicrobiology (Reading, England) · 2026
    Article
  3. Article
  4. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 2 institutions in 3 countries.

Nobuyuki ShimohataInstitute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.
Shushi Nagamori
Yoshinori Akiyama
H Ronald Kaback
Koreaki Ito
Kyoto University · JPCzech Academy of Sciences, Institute of Physiology · CZ

Funding

NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Structural Basis for Mechanism of Secondary TransportersR01DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2005 to 2013
$3.7M
Structural Basis for Mechanism of Secondary TransportersR56DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2009 to 2009
$500k
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK069463NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R01 DK069463NIDDK NIH HHS R56 DK051131NIDDK NIH HHS R56 DK069463
6 · The paper itself

Abstract

We report on a class of Escherichia coli SecY mutants that impair membrane protein folding. The mutants also up-regulate the Cpx/sigma(E) stress response pathways. Similar stress induction was also observed in response to a YidC defect in membrane protein biogenesis but not in response to the signal recognition particle-targeting defect or in response to a simple reduction in the abundance of the translocon. Together with the previous contention that the Cpx system senses a protein abnormality not only at periplasmic and outer membrane locations but also at the plasma membrane, abnormal states of membrane proteins are postulated to be generated in these secY mutants. In support of this notion, in vitro translation, membrane integration, and folding of LacY reveal that mutant membrane vesicles allow the insertion of LacY but not subsequent folding into a normal conformation recognizable by conformation-specific antibodies. The results demonstrate that normal SecY function is required for the folding of membrane proteins after their insertion into the translocon.

Indexed as

Escherichia coliEscherichia coli ProteinsIntracellular MembranesMembrane ProteinsMonosaccharide Transport ProteinsMutagenesisProtein ConformationProtein FoldingProtein TransportSEC Translocation ChannelsSigma FactorSymportersTranscription FactorsUp-RegulationEscherichia coli ProteinsLacY protein, E coliMembrane ProteinsMonosaccharide Transport ProteinsSEC Translocation ChannelsSecY protein, E coliSigma Factorsporulation-specific sigma factorsSymportersTranscription Factors

Identifiers

PMID17242069
PMCPMC2063957
OpenAlexW2160595750

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.