Evidence map›Paper›PMID 40259657›Full record

ReviewThe FEBS journal2025

New insights into Sti1/Hop's cochaperone function highlight the complexity of proteostatic regulation.

Gregory Lloyd Blatch, Adrienne Lesley Edkins

Abstract readReview
In one paragraph

Review in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    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.

Gregory Lloyd BlatchThe Vice Chancellery, The University of Notre Dame Australia, Fremantle, Australia.
Adrienne Lesley EdkinsBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry, Microbiology and Bioinformatics, Rhodes University, Makhanda, South Africa.ORCID https://orcid.org/0000-0002-3615-6651

Funding

Academy of Medical Sciences NewtonAdvancedFellowshipDepartment of Science and Innovation/National Research Foundation South Africa 98566Foreign, Commonwealth and Development Office MR/V030701/1Global Health EDCTP3 Joint Undertaking (UKRI MRC) MR/V030701/1Medical Research Council MR/V030701/1Rhodes University IFRR100220
6 · The paper itself

Abstract

Sti1/Hop is a cochaperone that regulates Hsp70 and Hsp90 chaperones. Sti1/Hop function is perceived as limited to scaffolding chaperone complexes, although recent studies suggest a broader function. Rutledge et al. show that while Sti1/Hop functions within chaperone complexes under basal conditions, during high stress, it operates independently to sequester soluble misfolded protein in the cytoplasm, a function typically associated with chaperones rather than cochaperones. Furthermore, the localisation and levels of Sti1/Hop are finely tuned to ensure orderly sequestration and resolution of misfolded proteins. These data support a role for Sti1/Hop as a cochaperone specialised for stressed proteostasis networks.

Indexed as

Heat-Shock ProteinsMolecular ChaperonesProteostasisSaccharomyces cerevisiae ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansProtein FoldingSaccharomyces cerevisiaeHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSTI1 protein, S cerevisiaeHopSti1STIP1

Identifiers

PMID40259657
PMCPMC12265853

What OpenQuestion holds

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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.