Evidence map›Paper›PMID 25378400›Full record

ArticleThe Journal of biological chemistry2014

Aha1 can act as an autonomous chaperone to prevent aggregation of stressed proteins.

Vishwadeepak Tripathi, Stefanie Darnauer, Nadine R Hartwig, Wolfgang M J Obermann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024
    Review
  8. Human Aha1's N-terminal extension confers it holdase activity in vitro.Protein science : a publication of the Protein Society · 2023
    Article
  9. Article
  10. Aha1 Is an Autonomous Chaperone for SULT1A1.Chemical research in toxicology · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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.

Vishwadeepak TripathiFrom the Department of Cardiovascular Physiology, Ruhr-University Bochum, 44801 Bochum, Germany.
Stefanie DarnauerFrom the Department of Cardiovascular Physiology, Ruhr-University Bochum, 44801 Bochum, Germany.
Nadine R HartwigFrom the Department of Cardiovascular Physiology, Ruhr-University Bochum, 44801 Bochum, Germany.
Wolfgang M J ObermannFrom the Department of Cardiovascular Physiology, Ruhr-University Bochum, 44801 Bochum, Germany Wolfgang.Obermann@rub.de.
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aha1 (activator of Hsp90 ATPase) stimulates the ATPase activity of the molecular chaperone Hsp90 to accelerate the conformational cycle during which client proteins attain their final shape. Thereby, Aha1 promotes effective folding of Hsp90-dependent clients such as steroid receptors and many kinases involved in cellular signaling. In our current study, we find that Aha1 plays a novel, additional role beyond regulating the Hsp90 ATP hydrolysis rate. We propose a new concept suggesting that Aha1 acts as an autonomous chaperone and associates with stress-denatured proteins to prevent them from aggregation similar to the chaperonin GroEL. Our study reveals that an N-terminal sequence of 22 amino acids, present in human but absent from yeast Aha1, is critical for this capability. However, in lieu of fostering their refolding, Aha1 allows ubiquitination of bound clients by the E3 ubiquitin ligase CHIP. Accordingly, Aha1 may promote disposal of folding defective proteins by the cellular protein quality control.

Indexed as

AnimalsHEK293 CellsHSP90 Heat-Shock ProteinsHumansLuciferases, FireflyMacaca mulattaMiceMolecular ChaperonesProtein Aggregation, PathologicalProtein BindingProtein RefoldingProteolysisThiosulfate SulfurtransferaseUbiquitinationAHSA1 protein, humanHSP90 Heat-Shock ProteinsLuciferases, FireflyMolecular ChaperonesThiosulfate SulfurtransferaseActivator of Hsp90 ATPase (Aha1)ATPaseHeat Shock Protein 90 (Hsp90)Molecular ChaperoneProtein AggregationProtein Folding

Identifiers

PMID25378400
PMCPMC4276884
OpenAlexW2001081135

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.