Evidence map›Paper›PMID 15215316›Full record

ArticleMolecular biology of the cell2004

The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.

Simon Alberti, Karsten Böhse, Verena Arndt, Anton Schmitz, Jörg Höhfeld

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

83 citing papers in PubMed, 178 citations in OpenAlex.

  1. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  2. Review
  3. Article
  4. Functional Consequences of CFTR Interactions in Cystic Fibrosis.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Distribution, expression of hexaploid wheatFrontiers in plant science · 2022
    Article
  11. Article
  12. Revisiting CFTR Interactions: Old Partners and New Players.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

23 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Simon AlbertiInstitut für Zellbiologie and Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn, D-53121 Bonn, Germany.
Karsten Böhse
Verena Arndt
Anton Schmitz
Jörg Höhfeld
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The CHIP ubiquitin ligase turns molecular chaperones into protein degradation factors. CHIP associates with the chaperones Hsc70 and Hsp90 during the regulation of signaling pathways and during protein quality control, and directs chaperone-bound clients to the proteasome for degradation. Obviously, this destructive activity should be carefully controlled. Here, we identify the cochaperone HspBP1 as an inhibitor of CHIP. HspBP1 attenuates the ubiquitin ligase activity of CHIP when complexed with Hsc70. As a consequence, HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation. Our data reveal a novel regulatory mechanism that determines folding and degradation activities of molecular chaperones.

Indexed as

Adaptor Proteins, Signal TransducingCarrier ProteinsCell LineCystic Fibrosis Transmembrane Conductance RegulatorHeLa CellsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansIn Vitro TechniquesModels, BiologicalMolecular ChaperonesMultiprotein ComplexesProtein FoldingRecombinant ProteinsUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingCarrier ProteinsCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA8 protein, humanHSPBP1 protein, humanMolecular ChaperonesMultiprotein ComplexesRecombinant ProteinsSTUB1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID15215316
PMCPMC515335
OpenAlexW2116511323

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.