Evidence map›Paper›PMID 30366631›Full record

ArticleBiophysical journal2018

Forces on Nascent Polypeptides during Membrane Insertion and Translocation via the Sec Translocon.

Michiel J M Niesen, Annika Müller-Lucks, Rickard Hedman, Gunnar von Heijne, Thomas F Miller

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  5. Cotranslational folding and assembly of the dimericProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Review
  10. Membrane protein folding and quality control.Current opinion in structural biology · 2021
    Review
  11. Article
  12. Local Bilayer Hydrophobicity Modulates Membrane Protein Stability.Journal of the American Chemical Society · 2021
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Structural insight into co-translational membrane protein folding.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  20. 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

5 authors.

Michiel J M NiesenDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California.
Annika Müller-LucksDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Rickard HedmanDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Gunnar von HeijneDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Thomas F MillerDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California. Electronic address: tfm@caltech.edu.

Funding

A New Pradigm for the Rational Expression of Integral Membrane ProteinsR01GM125063 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CLEMONS, WILLIAM M., MILLER, THOMAS FRANCIS · 2017 to 2020
$1.5M
NIGMS NIH HHS R01 GM125063
6 · The paper itself

Abstract

During ribosomal translation, nascent polypeptide chains (NCs) undergo a variety of physical processes that determine their fate in the cell. This study utilizes a combination of arrest peptide experiments and coarse-grained molecular dynamics to measure and elucidate the molecular origins of forces that are exerted on NCs during cotranslational membrane insertion and translocation via the Sec translocon. The approach enables deconvolution of force contributions from NC-translocon and NC-ribosome interactions, membrane partitioning, and electrostatic coupling to the membrane potential. In particular, we show that forces due to NC-lipid interactions provide a readout of conformational changes in the Sec translocon, demonstrating that lateral gate opening only occurs when a sufficiently hydrophobic segment of NC residues reaches the translocon. The combination of experiment and theory introduced here provides a detailed picture of the molecular interactions and conformational changes during ribosomal translation that govern protein biogenesis.

Indexed as

Cell MembraneMolecular Dynamics SimulationPeptidesProtein ConformationProtein TransportSEC Translocation ChannelsPeptidesSEC Translocation Channels

Identifiers

PMID30366631
PMCPMC6303271

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.