Evidence map›Paper›PMID 17220467›Full record

ArticleEukaryotic cell2007

Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p).

Patricija Hawle, Danielle Horst, Jan Paul Bebelman, Xiao Xian Yang, Marco Siderius, Saskia M van der Vies

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Organismal Roles of Hsp90.Biomolecules · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Azole resistance in aThe Journal of biological chemistry · 2018
    Article
  12. Article
  13. Article
  14. Stress Adaptation.Microbiology spectrum · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

6 authors at 1 institution in 1 country.

Patricija HawleDepartment of Biochemistry and Molecular Biology, Faculty of Science, Vrije Universiteit, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands.
Danielle Horst
Jan Paul Bebelman
Xiao Xian Yang
Marco Siderius
Saskia M van der Vies
Vrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast Saccharomyces cerevisiae utilizes rapidly responding mitogen-activated protein kinase (MAPK) signaling cascades to adapt efficiently to a changing environment. Here we report that phosphorylation of Cdc37p, an Hsp90 cochaperone, by casein kinase 2 controls the functionality of two MAPK cascades in yeast. These pathways, the high-osmolarity glycerol (HOG) pathway and the cell integrity (protein kinase C) MAPK pathway, mediate adaptive responses to high osmotic and cell wall stresses, respectively. Mutation of the phosphorylation site Ser14 in Cdc37p renders cells sensitive to osmotic stress and cell wall perturbation by calcofluor white. We found that levels of the MAPKs Hog1p and Slt2p (Mpk1p) in cells are reduced in a cdc37-S14A mutant, and consequently downstream responses mediated by Hog1p and Slt2p are compromised. Furthermore, we present evidence that Hog1p and Slt2p both interact in a complex with Cdc37p in vivo, something that has not been reported previously. The interaction of Hsp90, Slt2p, and Hog1p with Cdc37p depends on the phosphorylation status of Cdc37p. In fact, our biochemical data show that the osmosensitive phenotype of the cdc37-S14A mutant is due to the loss of the interaction between Cdc37p, Hog1p, and Hsp90. Likewise, during cell wall stress, the interaction of Slt2p with Cdc37p and Hsp90 is crucial for Slt2p-dependent downstream responses, such as the activation of the transcription factor Rlm1p. Interestingly, phosphorylated Slt2p, but not phosphorylated Hog1p, has an increased affinity for Cdc37p. Together these observations suggest that Cdc37p acts as a regulator of MAPK signaling.

Indexed as

Cell Cycle ProteinsCell WallGene Expression Regulation, FungalGlycerolHSP90 Heat-Shock ProteinsMADS Domain ProteinsMitogen-Activated Protein KinasesMolecular ChaperonesOsmotic PressurePhosphorylationProtein Kinase CSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsCDC37 protein, S cerevisiaeCell Cycle ProteinsGlycerolHOG1 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMADS Domain ProteinsMitogen-Activated Protein KinasesMolecular ChaperonesProtein Kinase CRLM1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLT2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID17220467
PMCPMC1828922
OpenAlexW2145512007

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.