Evidence map›Paper›PMID 34211117›Full record

ArticleCommunications biology2021

An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum.

Sarah O'Keefe, Guanghui Zong, Kwabena B Duah, Lauren E Andrews, Wei Q Shi, Stephen High

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. 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
6.4field-weighted citation impact, top 2% 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, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. TheeLife · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  13. Article
  14. Article
  15. EMC rectifies the topology of multipass membrane proteins.Nature structural & molecular biology · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. The Biogenesis of Multipass Membrane Proteins.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

6 authors at 4 institutions in 2 countries.

Sarah O'KeefeSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK. sarah.okeefe@manchester.ac.uk.ORCID http://orcid.org/0000-0002-1744-0198
Guanghui ZongDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD, USA.ORCID http://orcid.org/0000-0002-7335-039X
Kwabena B DuahDepartment of Chemistry, Ball State University, Muncie, IN, USA.
Lauren E AndrewsDepartment of Chemistry, Ball State University, Muncie, IN, USA.
Wei Q ShiDepartment of Chemistry, Ball State University, Muncie, IN, USA.ORCID http://orcid.org/0000-0001-5453-1753
Stephen HighSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK. stephen.high@manchester.ac.uk.ORCID http://orcid.org/0000-0002-4532-8152
Ball State University · USManchester Academic Health Science Centre · GBUniversity of Manchester · GBUniversity of Maryland, College Park · US

Funding

Medicinal Chemistry and Chemical Proteomics of Ipomoeassin Natural GlycoresinsR15GM116032 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI SHI, WEI · 2015 to 2020
$767k
NIGMS NIH HHS R15 GM116032Wellcome Trust 204957/Z/16/Z
6 · The paper itself

Abstract

The heterotrimeric Sec61 complex is a major site for the biogenesis of transmembrane proteins (TMPs), accepting nascent TMP precursors that are targeted to the endoplasmic reticulum (ER) by the signal recognition particle (SRP). Unlike most single-spanning membrane proteins, the integration of type III TMPs is completely resistant to small molecule inhibitors of the Sec61 translocon. Using siRNA-mediated depletion of specific ER components, in combination with the potent Sec61 inhibitor ipomoeassin F (Ipom-F), we show that type III TMPs utilise a distinct pathway for membrane integration at the ER. Hence, following SRP-mediated delivery to the ER, type III TMPs can uniquely access the membrane insertase activity of the ER membrane complex (EMC) via a mechanism that is facilitated by the Sec61 translocon. This alternative EMC-mediated insertion pathway allows type III TMPs to bypass the Ipom-F-mediated blockade of membrane integration that is seen with obligate Sec61 clients.

Indexed as

Protein BiosynthesisAnimalsEndoplasmic ReticulumGlycoconjugatesHeLa CellsHumansImmunoblottingIntracellular MembranesMembrane ProteinsModels, BiologicalProtein TransportRNA InterferenceSEC Translocation ChannelsSignal Recognition ParticleGlycoconjugatesipomoeassin FMembrane ProteinsSEC Translocation ChannelsSignal Recognition Particle

Identifiers

PMID34211117
PMCPMC8249459
OpenAlexW3173719914

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.