Evidence map›Paper›PMID 24561504›Full record

ArticleNature structural & molecular biology2014

Cotranslational folding inhibits translocation from within the ribosome-Sec61 translocon complex.

Brian J Conti, Johannes Elferich, Zhongying Yang, Ujwal Shinde, William R Skach

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Protein folding in the cell, from atom to organism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  15. 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 at 1 institution in 1 country.

Brian J ContiDepartment of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, Oregon, USA.
Johannes ElferichDepartment of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, Oregon, USA.
Zhongying YangDepartment of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, Oregon, USA.
Ujwal ShindeDepartment of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, Oregon, USA.
William R SkachDepartment of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, Oregon, USA.
Oregon Health & Science University · US

Funding

Multidisciplinary Research Training in Pulmonary MedicineT32HL083808 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LEWINSOHN, DAVID M., SLATORE, CHRISTOPHER G. · 2008 to 2025
$5.3M
MECHANISMS OF POLYTOPIC PROTEIN BIOGENESIS IN THE ERR01GM053457 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SKACH, WILLIAM R · 1996 to 2013
$3.5M
BIOGENESIS AND MOLECULAR PATHOGENESIS OF CFTRR01DK051818 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI SKACH, WILLIAM R · 1997 to 2012
$2.9M
Mechanisms of Sec61-Mediated Polytopic Protein Integration into the ERF32GM083568 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI CONTI, BRIAN J · 2008 to 2009
$101k
NHLBI NIH HHS T32 HL083808NIDDK NIH HHS DK51818NIDDK NIH HHS R01 DK051818NIGMS NIH HHS F32 GM083568NIGMS NIH HHS GM53457NIGMS NIH HHS R01 GM053457
6 · The paper itself

Abstract

Eukaryotic secretory proteins cross the endoplasmic reticulum (ER) membrane through a protein-conducting channel contained within the ribosome-Sec61translocon complex (RTC). Using a zinc-finger sequence as a folding switch, we show that cotranslational folding of a secretory passenger inhibits translocation in canine ER microsomes and in human cells. Folding occurs within a cytosolically inaccessible environment, after ER targeting but before initiation of translocation, and it is most effective when the folded domain is 15-54 residues beyond the signal sequence. Under these conditions, substrate is diverted into cytosol at the stage of synthesis in which unfolded substrate enters the ER lumen. Moreover, the translocation block is reversed by passenger unfolding even after cytosol emergence. These studies identify an enclosed compartment within the assembled RTC that allows a short span of nascent chain to reversibly abort translocation in a substrate-specific manner.

Indexed as

Protein BiosynthesisAnimalsCell LineCytosolDogsEndopeptidase KEndoplasmic ReticulumHEK293 CellsHumansKineticsMembrane Transport ProteinsMicrosomesPlasmidsProtein BindingProtein ConformationProtein FoldingEndopeptidase KMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation ChannelsZinc

Identifiers

PMID24561504
PMCPMC4351553
OpenAlexW2002696824

What OpenQuestion holds

Textmetadata
LicenceTDM
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.