Evidence map›Paper›PMID 25053410›Full record

ArticleThe Journal of biological chemistry2014

The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.

Katharina Papsdorf, Julia Sacherl, Klaus Richter

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Temperature Effects on Expression Levels ofInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. HLH-1 Modulates Muscle Proteostasis DuringFrontiers in cell and developmental biology · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The nucleotide exchange factors of Hsp70 molecular chaperones.Frontiers in molecular biosciences · 2015
    Review
  14. 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

3 authors at 1 institution in 1 country.

Katharina PapsdorfFrom the Department of Biotechnology and Center for Integrated Protein Science Munich (CIPS), Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Julia SacherlFrom the Department of Biotechnology and Center for Integrated Protein Science Munich (CIPS), Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany.
Klaus RichterFrom the Department of Biotechnology and Center for Integrated Protein Science Munich (CIPS), Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany klaus.richter@richterlab.de.
Center for Integrated Protein Science Munich · DE

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

The molecular chaperone Hsc70 assists in the folding of non-native proteins together with its J domain- and BAG domain-containing cofactors. In Caenorhabditis elegans, two BAG domain-containing proteins can be identified, one of them being UNC-23, whose mutation induces severe motility dysfunctions. Using reporter strains, we find that the full-length UNC-23, in contrast to C-terminal fragments, localizes specifically to the muscular attachment sites. C-terminal fragments of UNC-23 instead perform all Hsc70-related functions, like ATPase stimulation and regulation of folding activity, albeit with lower affinity than BAG-1. Interestingly, overexpression of CFP-Hsc70 can induce muscular defects in wild-type nematodes that phenocopy the knockout of its cofactor UNC-23. Strikingly, the motility dysfunction in the unc-23 mutated strain can be cured specifically by down-regulation of the antagonistic Hsc70 cochaperone DNJ-13, implying that the severe phenotype is caused by misregulation of the Hsc70 cycle. These findings point out that the balanced action of cofactors in the ATP-driven cycle of Hsc70 is crucial for the contribution of Hsc70 to muscle functionality.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsCarrier ProteinsHSC70 Heat-Shock ProteinsLuminescent ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceMotor ActivityMusclesMutationAdenosine TriphosphatasesAdenosine TriphosphateCaenorhabditis elegans ProteinsCarrier ProteinsHSC70 Heat-Shock ProteinsLuminescent Proteinsphorbol ester binding proteinBag2Caenorhabditis elegans (C. elegans)Heat Shock Protein (HSP)Molecular ChaperoneMuscular DystrophyShear Stress

Identifiers

PMID25053410
PMCPMC4155687
OpenAlexW1976758764

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.