Evidence map›Paper›PMID 12475939›Full record

ArticleMolecular biology of the cell2002

Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein.

Suzanna L Meacock, Fabienne J L Lecomte, Samuel G Crawshaw, Stephen High

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 92 citations in OpenAlex.

  1. SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
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  6. Article
  7. Article
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  10. Review
  11. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  12. Review
  13. Article
  14. The enigmatic ATP supply of the endoplasmic reticulum.Biological reviews of the Cambridge Philosophical Society · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015
    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

4 authors at 1 institution in 1 country.

Suzanna L MeacockSchool of Biological Sciences, University of Manchester, Manchester, M13 9PT United Kingdom.
Fabienne J L Lecomte
Samuel G Crawshaw
Stephen High
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council SF16973
6 · The paper itself

Abstract

We have been studying the insertion of the seven transmembrane domain (TM) protein opsin to gain insights into how the multiple TMs of polytopic proteins are integrated at the endoplasmic reticulum (ER). We find that the ER components associated with the first and second TMs of the nascent opsin polypeptide chain are clearly distinct. The first TM (TM1) is adjacent to the alpha and beta subunits of the Sec61 complex, and a novel component, a protein associated with the ER translocon of 10 kDa (PAT-10). The most striking characteristic of PAT-10 is that it remains adjacent to TM1 throughout the biogenesis and membrane integration of the full-length opsin polypeptide. TM2 is also found to be adjacent to Sec61alpha and Sec61beta during its membrane integration. However, TM2 does not form any adducts with PAT-10; rather, a transient association with the TRAM protein is observed. We show that the association of PAT-10 with opsin TM1 does not require the N-glycosylation of the nascent chain and occurs irrespective of the amino acid sequence and transmembrane topology of TM1. We conclude that the precise makeup of the ER membrane insertion site can be distinct for the different transmembrane domains of a polytopic protein. We find that the environment of a particular TM can be influenced by both the "stage" of nascent chain biosynthesis reached, and the TM's relative location within the polypeptide.

Indexed as

Membrane GlycoproteinsReceptors, Cytoplasmic and NuclearAnimalsCattleCell MembraneCross-Linking ReagentsDogsEndoplasmic ReticulumGlycosylationMembrane ProteinsMicrosomesModels, BiologicalMolecular ChaperonesMutagenesis, Site-DirectedNeurotensinPancreasCross-Linking ReagentsMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesNeurotensinProtein IsoformsReceptors, Cytoplasmic and NuclearReceptors, PeptideRod OpsinsSEC Translocation Channels

Identifiers

PMID12475939
PMCPMC138620
OpenAlexW2158475730

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.