Evidence map›Paper›PMID 14742721›Full record

ArticleMolecular biology of the cell2004

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

Paul Lee, Arsalan Shabbir, Christopher Cardozo, Avrom J Caplan

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 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 86 citations in OpenAlex.

  1. Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024
    Review
  2. Article
  3. Article
  4. Detecting Posttranslational Modifications of Hsp90 Isoforms.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
  6. Review
  7. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  8. Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019
    Review
  9. Detecting Posttranslational Modifications of Hsp90.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Detecting HSP90 phosphorylation.Methods in molecular biology (Clifton, N.J.) · 2011
    Article
  20. 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

4 authors at 1 institution in 1 country.

Paul LeeDepartment of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, New York 10029, USA.
Arsalan Shabbir
Christopher Cardozo
Avrom J Caplan
Icahn School of Medicine at Mount Sinai · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp90 functions in association with several cochaperones for folding of protein kinases and transcription factors, although the relative contribution of each to the overall reaction is unknown. We assayed the role of nine different cochaperones in the activation of Ste11, a Saccharomyces cerevisiae mitogen-activated protein kinase kinase kinase. Studies on signaling via this protein kinase pathway was measured by alpha-factor-stimulated induction of FIG1 or lacZ, and repression of HHF1. Several cochaperone mutants tested had reduced FIG1 induction or HHF1 repression, although to differing extents. The greatest defects were in cpr7Delta, sse1Delta, and ydj1Delta mutants. Assays of Ste11 kinase activity revealed a pattern of defects in the cochaperone mutant strains that were similar to the gene expression studies. Overexpression of CDC37, a chaperone required for protein kinase folding, suppressed defects the sti1Delta mutant back to wild-type levels. CDC37 overexpression also restored stable Hsp90 binding to the Ste11 protein kinase domain in the sti1Delta mutant strain. These data suggest that Cdc37 and Sti1 have functional overlap in stabilizing Hsp90:client complexes. Finally, we show that Cns1 functions in MAP kinase signaling in association with Cpr7.

Indexed as

Blotting, WesternCarrier ProteinsCell Cycle ProteinsDrosophila ProteinsFungal ProteinsGene Expression RegulationHeat-Shock ProteinsHSP90 Heat-Shock ProteinsLac OperonMAP Kinase Kinase KinasesMAP Kinase Signaling SystemModels, BiologicalMolecular ChaperonesMutationPheromonesPlasmidsCarrier ProteinsCDC37 protein, S cerevisiaeCell Cycle ProteinsDrosophila ProteinsFungal ProteinsHeat-Shock ProteinsHSP90 Heat-Shock ProteinsMAP Kinase Kinase KinasesMolecular ChaperonesPheromonesRNASaccharomyces cerevisiae ProteinsSte11 protein, S cerevisiaeSTI1 protein, S cerevisiae

Identifiers

PMID14742721
PMCPMC379275
OpenAlexW2095686344

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.