Evidence map›Paper›PMID 37515325›Full record

ArticleBiophysical journal2023

Aha1 regulates Hsp90's conformation and function in a stoichiometry-dependent way.

Tanumoy Mondol, Laura-Marie Silbermann, Julia Schimpf, Leonie Vollmar, Bianca Hermann, Katarzyna Kasia Tych, Thorsten Hugel

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. VdAHA1 positively regulate pathogenicity inFrontiers in microbiology · 2025
    Article
  9. Review
  10. The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024
    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

7 authors at 2 institutions in 2 countries.

Tanumoy MondolInstitute of Physical Chemistry, University of Freiburg, Freiburg im Breisgau, Germany; Signalling Research Centers BIOSS and CIBSS, University of Freiburg, Freiburg im Breisgau, Germany.
Laura-Marie SilbermannGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
Julia SchimpfInstitute of Physical Chemistry, University of Freiburg, Freiburg im Breisgau, Germany; Signalling Research Centers BIOSS and CIBSS, University of Freiburg, Freiburg im Breisgau, Germany; Speemann Graduate School of Biology and Medicine, University of Freiburg, Freiburg im Breisgau, Germany.
Leonie VollmarInstitute of Physical Chemistry, University of Freiburg, Freiburg im Breisgau, Germany; Signalling Research Centers BIOSS and CIBSS, University of Freiburg, Freiburg im Breisgau, Germany; Speemann Graduate School of Biology and Medicine, University of Freiburg, Freiburg im Breisgau, Germany.
Bianca HermannInstitute of Physical Chemistry, University of Freiburg, Freiburg im Breisgau, Germany; Signalling Research Centers BIOSS and CIBSS, University of Freiburg, Freiburg im Breisgau, Germany.
Katarzyna Kasia TychGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands. Electronic address: k.m.tych@rug.nl.
Thorsten HugelInstitute of Physical Chemistry, University of Freiburg, Freiburg im Breisgau, Germany; Signalling Research Centers BIOSS and CIBSS, University of Freiburg, Freiburg im Breisgau, Germany. Electronic address: thorsten.hugel@pc.uni-freiburg.de.
University of Freiburg · DEUniversity of Groningen · NL

Funding

European Research Council 681891
6 · The paper itself

Abstract

The heat shock protein 90 (Hsp90) is a molecular chaperone, which plays a key role in eukaryotic protein homeostasis. Co-chaperones assist Hsp90 in client maturation and in regulating essential cellular processes such as cell survival, signal transduction, gene regulation, hormone signaling, and neurodegeneration. Aha1 (activator of Hsp90 ATPase) is a unique co-chaperone known to stimulate the ATP hydrolysis of Hsp90, but the mechanism of their interaction is still unclear. In this report, we show that one or two Aha1 molecules can bind to one Hsp90 dimer and that the binding stoichiometry affects Hsp90's conformation, kinetics, ATPase activity, and stability. In particular, a coordination of two Aha1 molecules can be seen in stimulating the ATPase activity of Hsp90 and the unfolding of the middle domain, whereas the conformational equilibrium and kinetics are hardly affected by the stoichiometry of bound Aha1. Altogether, we show a regulation mechanism through the stoichiometry of Aha1 going far beyond a regulation of Hsp90's conformation.

Indexed as

HSP90 Heat-Shock ProteinsMolecular ChaperonesAdenosine TriphosphatasesHumansMolecular ConformationAdenosine TriphosphatasesHSP90 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID37515325
PMCPMC10502475
OpenAlexW4385310334

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.