Evidence map›Paper›PMID 36096638›Full record

ReviewCold Spring Harbor perspectives in biology2023

The Biogenesis of Multipass Membrane Proteins.

Luka Smalinskaitė, Ramanujan S Hegde

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Review
  10. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  11. Article
  12. Review
  13. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. EMC rectifies the topology of multipass membrane proteins.Nature structural & molecular biology · 2024
    Article
  19. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    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

2 authors at 1 institution in 1 country.

Luka SmalinskaitėMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom rhegde@mrc-lmb.cam.ac.uk.ORCID 0000-0001-8338-852X
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_A022_1007
6 · The paper itself

Abstract

Multipass membrane proteins contain two or more α-helical transmembrane domains (TMDs) that span the lipid bilayer. They are inserted cotranslationally into the prokaryotic plasma membrane or eukaryotic endoplasmic reticulum membrane. The Sec61 complex (SecY complex in prokaryotes) provides a ribosome docking site, houses a channel across the membrane, and contains a lateral gate that opens toward the lipid bilayer. Model multipass proteins can be stitched into the membrane by iteratively using Sec61's lateral gate for TMD insertion and its central pore for translocation of flanking domains. Native multipass proteins, with their diverse TMDs and complex topologies, often also rely on members of the Oxa1 family of translocation factors, the PAT complex chaperone, and other poorly understood factors. Here, we discuss the mechanisms of TMD insertion, highlight the limitations of an iterative insertion model, and propose a new hypothesis for multipass membrane protein biogenesis based on recent findings.

Indexed as

Lipid BilayersMembrane ProteinsCell MembraneProtein TransportSEC Translocation ChannelsLipid BilayersMembrane ProteinsSEC Translocation Channels

Identifiers

PMID36096638
PMCPMC10071439
OpenAlexW4295420773

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.