Evidence map›Paper›PMID 25179605›Full record

ArticleJournal of cell science2014

SGTA regulates the cytosolic quality control of hydrophobic substrates.

Lydia Wunderley, Pawel Leznicki, Aishwarya Payapilly, Stephen High

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Mechanisms suppressing noncoding translation.Trends in cell biology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Frontiers in molecular biosciences · 2022
    Article
  12. Review
  13. Article
  14. Article
  15. The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019
    Review
  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.

Lydia WunderleyFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Pawel LeznickiFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Aishwarya PayapillyFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Stephen HighFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK stephen.high@manchester.ac.uk.
University of Manchester · GB

Funding

Wellcome TrustWellcome Trust 0881163/Z/09/ZWellcome Trust 092107/Z/10/ZWellcome Trust 093177/Z/10/A
6 · The paper itself

Abstract

Hydrophobic amino acids are normally shielded from the cytosol and their exposure is often used as an indicator of protein misfolding to enable the chaperone-mediated recognition and quality control of aberrant polypeptides. Mislocalised membrane proteins (MLPs) represent a particular challenge to cellular quality control, and, in this study, membrane protein fragments have been exploited to study a specialised pathway that underlies the efficient detection and proteasomal degradation of MLPs. Our data show that the BAG6 complex and SGTA compete for cytosolic MLPs by recognition of their exposed hydrophobicity, and the data suggest that SGTA acts to maintain these substrates in a non-ubiquitylated state. Hence, SGTA might counter the actions of BAG6 to delay the ubiquitylation of specific precursors and thereby increase their opportunity for successful post-translational delivery to the endoplasmic reticulum. However, when SGTA is overexpressed, the normally efficient removal of aberrant MLPs is delayed, increasing their steady-state level and promoting aggregation. Our data suggest that SGTA regulates the cellular fate of a range of hydrophobic polypeptides should they become exposed to the cytosol.

Indexed as

Blotting, WesternCarrier ProteinsCytosolHeLa CellsHumansHydrophobic and Hydrophilic InteractionsImmunoprecipitationMembrane ProteinsMicroscopy, FluorescenceMolecular ChaperonesCarrier ProteinsMembrane ProteinsMolecular ChaperonesSGTA protein, humanAggresomesBAG6Mislocalised membrane proteinsPolyubiquitylationProtein degradationSmall glutamine-rich tetratricopeptide repeat-containing protein alpha

Identifiers

PMID25179605
PMCPMC4215715
OpenAlexW2002149580

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.