Evidence map›Paper›PMID 16778768›Full record

ArticleThe EMBO journal2006

Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway.

Kazuo Tatebayashi, Katsuyoshi Yamamoto, Keiichiro Tanaka, Taichiro Tomida, Takashi Maruoka, Eri Kasukawa, Haruo Saito

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
4.9field-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

92 citing papers in PubMed, 170 citations in OpenAlex.

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  20. HJournal of fungi (Basel, Switzerland) · 2021
    Article

32 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

7 authors at 2 institutions in 1 country.

Kazuo TatebayashiDivision of Molecular Cell Signaling, Institute of Medical Sciences, University of Tokyo, Tokyo, Japan.
Katsuyoshi Yamamoto
Keiichiro Tanaka
Taichiro Tomida
Takashi Maruoka
Eri Kasukawa
Haruo Saito
The University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast high osmolarity glycerol (HOG) signaling pathway can be activated by either of the two upstream pathways, termed the SHO1 and SLN1 branches. When stimulated by high osmolarity, the SHO1 branch activates an MAP kinase module composed of the Ste11 MAPKKK, the Pbs2 MAPKK, and the Hog1 MAPK. To investigate how osmostress activates this MAPK module, we isolated both gain-of-function and loss-of-function alleles in four key genes involved in the SHO1 branch, namely SHO1, CDC42, STE50, and STE11. These mutants were characterized using an HOG-dependent reporter gene, 8xCRE-lacZ. We found that Cdc42, in addition to binding and activating the PAK-like kinases Ste20 and Cla4, binds to the Ste11-Ste50 complex to bring activated Ste20/Cla4 to their substrate Ste11. Activated Ste11 and its HOG pathway-specific substrate, Pbs2, are brought together by Sho1; the Ste11-Ste50 complex binds to the cytoplasmic domain of Sho1, to which Pbs2 also binds. Thus, Cdc42, Ste50, and Sho1 act as adaptor proteins that control the flow of the osmostress signal from Ste20/Cla4 to Ste11, then to Pbs2.

Indexed as

cdc42 GTP-Binding Protein, Saccharomyces cerevisiaeEnzyme ActivationGenes, ReporterGlycerolIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMAP Kinase Signaling SystemMembrane ProteinsMitogen-Activated Protein Kinase KinasesModels, MolecularMutationOsmolar ConcentrationOsmotic PressureProtein BindingProtein Serine-Threonine KinasesSaccharomyces cerevisiaecdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCLA4 protein, S cerevisiaeGlycerolIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMembrane ProteinsMitogen-Activated Protein Kinase KinasesPBS2 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSHO1 protein, S cerevisiaeSte11 protein, S cerevisiaeSTE20 protein, S cerevisiaeSTE50 protein, S cerevisiae

Identifiers

PMID16778768
PMCPMC1500976
OpenAlexW2084303011

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.