Evidence map›Paper›PMID 31575659›Full record

ReviewThe Journal of biological chemistry2019

Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade.

Shu-Ou Shan

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  19. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  20. 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

1 author at 1 institution in 1 country.

Shu-Ou ShanDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125 sshan@caltech.edu.ORCID 0000-0002-6526-1733
California Institute of Technology · US

Funding

Supplement: Accurate Molecular Decision Making during Protein BiogenesisR35GM136321 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Shu-ou Shan · 2020 to 2026
$6.7M
Molecular mechanisms of post-translational targeting of tail-anchored proteins.R01GM107368 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2014 to 2019
$2.1M
NIGMS NIH HHS R01 GM107368NIGMS NIH HHS R35 GM136321
6 · The paper itself

Abstract

Newly synthesized integral membrane proteins must traverse the aqueous cytosolic environment before arrival at their membrane destination and are prone to aggregation, misfolding, and mislocalization during this process. The biogenesis of integral membrane proteins therefore poses acute challenges to protein homeostasis within a cell and requires the action of effective molecular chaperones. Chaperones that mediate membrane protein targeting not only need to protect the nascent transmembrane domains from improper exposure in the cytosol, but also need to accurately select client proteins and actively guide their clients to the appropriate target membrane. The mechanisms by which cellular chaperones work together to coordinate this complex process are only beginning to be delineated. Here, we summarize recent advances in studies of the tail-anchored membrane protein targeting pathway, which revealed a network of chaperones, cochaperones, and targeting factors that together drive and regulate this essential process. This pathway is emerging as an excellent model system to decipher the mechanism by which molecular chaperones overcome the multiple challenges during post-translational membrane protein biogenesis and to gain insights into the functional organization of multicomponent chaperone networks.

Indexed as

Endoplasmic ReticulumHSP70 Heat-Shock ProteinsHumansMembrane ProteinsMolecular ChaperonesProtein BiosynthesisProtein DomainsRibosomesHSP70 Heat-Shock ProteinsMembrane ProteinsMolecular Chaperones70 kilodalton heat shock protein (Hsp70)ATPasechaperonemembrane proteinprotein targetingtail-anchored protein

Identifiers

PMID31575659
PMCPMC6851334
OpenAlexW2979161746

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.