Evidence map›Paper›PMID 26944342›Full record

ArticleMolecular & cellular proteomics : MCP2016

Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.

Michal Durech, Filip Trcka, Petr Man, Elizabeth A Blackburn, Lenka Hernychova, Petra Dvorakova, Dominika Coufalova, Daniel Kavan, Borivoj Vojtesek, Petr Muller

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
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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

10 authors at 3 institutions in 3 countries.

Michal DurechFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic;
Filip TrckaFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic;
Petr Man¶Institute of Microbiology, The Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic; ‖Department of Biochemistry, Faculty of Science, Charles University in Prague, Hlavova 8, 128 43 Prague, Czech Republic;
Elizabeth A Blackburn**Centre for Translational and Chemical Biology, Institute of Structural and Molecular Biology, University of Edinburgh, Max Born Crescent, The King's Buildings, Edinburgh EH9 3JR, United Kingdom.
Lenka HernychovaFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic;
Petra DvorakovaFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic;
Dominika CoufalovaFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic;
Daniel Kavan¶Institute of Microbiology, The Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic; ‖Department of Biochemistry, Faculty of Science, Charles University in Prague, Hlavova 8, 128 43 Prague, Czech Republic;
Borivoj VojtesekFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic; vojtesek@mou.cz muller@mou.cz.
Petr MullerFrom the ‡Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Zluty Kopec 7, 656 53 Brno, Czech Republic; vojtesek@mou.cz muller@mou.cz.
Masaryk Memorial Cancer Institute · CZCzech Academy of Sciences, Institute of Microbiology · CZInstitute of Structural and Molecular Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Co-chaperones containing tetratricopeptide repeat (TPR) domains enable cooperation between Hsp70 and Hsp90 to maintain cellular proteostasis. Although the details of the molecular interactions between some TPR domains and heat shock proteins are known, we describe a novel mechanism by which Tomm34 interacts with and coordinates Hsp70 activities. In contrast to the previously defined Hsp70/Hsp90-organizing protein (Hop), Tomm34 interaction is dependent on the Hsp70 chaperone cycle. Tomm34 binds Hsp70 in a complex process; anchorage of the Hsp70 C terminus by the TPR1 domain is accompanied by additional contacts formed exclusively in the ATP-bound state of Hsp70 resulting in a high affinity entropically driven interaction. Tomm34 induces structural changes in determinants within the Hsp70-lid subdomain and modulates Hsp70/Hsp40-mediated refolding and Hsp40-stimulated Hsp70 ATPase activity. Because Tomm34 recruits Hsp90 through its TPR2 domain, we propose a model in which Tomm34 enables Hsp70/Hsp90 scaffolding and influences the Hsp70 chaperone cycle, providing an additional role for co-chaperones that contain multiple TPR domains in regulating protein homeostasis.

Indexed as

Adenosine TriphosphateBinding SitesCrystallography, X-RayHSP70 Heat-Shock ProteinsHumansMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsModels, MolecularMolecular Docking SimulationMutationProtein BindingProtein FoldingProtein Structure, TertiaryAdenosine TriphosphateHSP70 Heat-Shock ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsTOMM34 protein, human

Identifiers

PMID26944342
PMCPMC4858950
OpenAlexW2345138467

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.