Evidence map›Paper›PMID 23401005›Full record

ArticleThe Journal of cell biology2013

SecYEG activates GTPases to drive the completion of cotranslational protein targeting.

David Akopian, Kush Dalal, Kuang Shen, Franck Duong, Shu-ou Shan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.0field-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

34 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021
    Review
  7. To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021
    Review
  8. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. The SRP signal sequence of KdpD.Scientific reports · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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 2 countries.

David AkopianDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Kush Dalal
Kuang Shen
Franck Duong
Shu-ou Shan
California Institute of Technology · USUniversity of British Columbia · CA

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Molecular Mechanism of Protein Targeting by the Signal Recognition ParticleR01GM078024 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2007 to 2020
$4.4M
NIGMS NIH HHS 5T32GM07616NIGMS NIH HHS GM078024NIGMS NIH HHS R01 GM078024NIGMS NIH HHS T32 GM007616
6 · The paper itself

Abstract

Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the translating ribosome or actively regulates this targeting machinery remains unclear. Here we show that SecYEG drives conformational changes in the cargo-loaded SRP-SR targeting complex that activate it for GTP hydrolysis and for handover of the translating ribosome. These results provide the first evidence that SecYEG actively drives the efficient delivery and unloading of translating ribosomes at the target membrane.

Indexed as

Models, BiologicalEscherichia coliEscherichia coli ProteinsGuanosine TriphosphateHydrolysisProtein Structure, TertiaryProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideRibosomesSEC Translocation ChannelsSignal Recognition ParticleEscherichia coli ProteinsGuanosine TriphosphateReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation Channelssignal peptide receptorSignal Recognition Particle

Identifiers

PMID23401005
PMCPMC3575545
OpenAlexW2106445116

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.