Evidence map›Paper›PMID 18166653›Full record

ArticleThe Journal of cell biology2007

Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis.

Yuichiro Kida, Fumiko Morimoto, Masao Sakaguchi

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015
    Review
  4. Review
  5. Article
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  7. In vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Cellular mechanisms of membrane protein folding.Nature structural & molecular biology · 2009
    Article
  18. Article
  19. Lipid-dependent membrane protein topogenesis.Annual review of biochemistry · 2009
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Yuichiro KidaGraduate School of Life Science, University of Hyogo, Hyogo 678-1297, Japan.
Fumiko Morimoto
Masao Sakaguchi
University of Hyogo · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During protein integration into the endoplasmic reticulum, the N-terminal domain preceding the type I signal-anchor sequence is translocated through a translocon. By fusing a streptavidin-binding peptide tag to the N terminus, we created integration intermediates of multispanning membrane proteins. In a cell-free system, N-terminal domain (N-domain) translocation was arrested by streptavidin and resumed by biotin. Even when N-domain translocation was arrested, the second hydrophobic segment mediated translocation of the downstream hydrophilic segment. In one of the defined intermediates, two hydrophilic segments and two hydrophobic segments formed a transmembrane disposition in a productive state. Both of the translocating hydrophilic segments were crosslinked with a translocon subunit, Sec61alpha. We conclude that two translocating hydrophilic segment in a single membrane protein can span the membrane during multispanning topogenesis flanking the translocon. Furthermore, even after six successive hydrophobic segments entered the translocon, N-domain translocation could be induced to restart from an arrested state. These observations indicate the remarkably flexible nature of the translocon.

Indexed as

AnimalsCell-Free SystemEndoplasmic ReticulumHumansHydrophobic and Hydrophilic InteractionsIntracellular MembranesMembrane ProteinsMolecular ChaperonesProtein BiosynthesisProtein ConformationProtein FoldingProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportSEC Translocation ChannelsMembrane ProteinsMolecular ChaperonesSEC61A1 protein, humanSEC Translocation Channels

Identifiers

PMID18166653
PMCPMC2373506
OpenAlexW2088552624

What OpenQuestion holds

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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.