Evidence map›Paper›PMID 25792736›Full record

ArticleThe Journal of biological chemistry2015

Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.

Lena Böttinger, Silke Oeljeklaus, Bernard Guiard, Sabine Rospert, Bettina Warscheid, Thomas Becker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Review
  3. HSP90α lactylation orchestrates PGC1α and LRPGC1 nuclear translocation driving mitochondrial biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  14. Biomolecules · 2022
    Article
  15. Mitochondrial chaperones in human health and disease.Free radical biology & medicine · 2022
    Review
  16. Review
  17. Article
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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

6 authors at 2 institutions in 2 countries.

Lena BöttingerFrom the Institut für Biochemie und Molekularbiologie, ZBMZ, the Fakultät für Biologie.
Silke OeljeklausInstitut für Biologie II, Abteilung Biochemie und Funktionelle Proteomik, Universität Freiburg, 79104 Freiburg, Germany, the BIOSS Centre for Biological Signalling Studies, and.
Bernard Guiardthe Centre de Génétique Moléculaire, CNRS, 91190 Gif-sur-Yvette, France.
Sabine RospertFrom the Institut für Biochemie und Molekularbiologie, ZBMZ, the BIOSS Centre for Biological Signalling Studies, and.
Bettina WarscheidInstitut für Biologie II, Abteilung Biochemie und Funktionelle Proteomik, Universität Freiburg, 79104 Freiburg, Germany, the BIOSS Centre for Biological Signalling Studies, and.
Thomas BeckerFrom the Institut für Biochemie und Molekularbiologie, ZBMZ, the Fakultät für Biologie, the BIOSS Centre for Biological Signalling Studies, and thomas.becker@biochemie.uni-freiburg.de.
Centre National de la Recherche Scientifique · FRUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial Hsp70 (mtHsp70) mediates essential functions for mitochondrial biogenesis, like import and folding of proteins. In these processes, the chaperone cooperates with cochaperones, the presequence translocase, and other chaperone systems. The chaperonin Hsp60, together with its cofactor Hsp10, catalyzes folding of a subset of mtHsp70 client proteins. Hsp60 forms heptameric ring structures that provide a cavity for protein folding. How the Hsp60 rings are assembled is poorly understood. In a comprehensive interaction study, we found that mtHsp70 associates with Hsp60 and Hsp10. Surprisingly, mtHsp70 interacts with Hsp10 independently of Hsp60. The mtHsp70-Hsp10 complex binds to the unassembled Hsp60 precursor to promote its assembly into mature Hsp60 complexes. We conclude that coupling to Hsp10 recruits mtHsp70 to mediate the biogenesis of the heptameric Hsp60 rings.

Indexed as

AnimalsChaperonin 10Chaperonin 60HSP70 Heat-Shock ProteinsMitochondriaSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChaperonin 10Chaperonin 60HSP70 Heat-Shock ProteinsSaccharomyces cerevisiae Proteins70-kDa Heat Shock Protein (Hsp70)Hsp10Hsp60MitochondriaMolecular ChaperoneProtein AssemblyProtein BiogenesisProtein Folding

Identifiers

PMID25792736
PMCPMC4416864
OpenAlexW2078565740

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.