Evidence map›Paper›PMID 26787842›Full record

ArticleMolecular and cellular biology2016

Scaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein Kinase.

Akiko Nishimura, Katsuyoshi Yamamoto, Masaaki Oyama, Hiroko Kozuka-Hata, Haruo Saito, Kazuo Tatebayashi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. HOG Signaling: A Multifunctional Regulator of Stress Homeostasis inJournal of fungi (Basel, Switzerland) · 2026
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  16. Stress Adaptation.Microbiology spectrum · 2017
    Review
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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 2 institutions in 1 country.

Akiko NishimuraDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
Katsuyoshi YamamotoDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Masaaki OyamaMedical Proteomics Laboratory, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Hiroko Kozuka-HataMedical Proteomics Laboratory, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Haruo SaitoDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan h-saito@ims.u-tokyo.ac.jp tategone@ims.u-tokyo.ac.jp.
Kazuo TatebayashiDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan h-saito@ims.u-tokyo.ac.jp tategone@ims.u-tokyo.ac.jp.
The University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the budding yeast Saccharomyces cerevisiae, osmostress activates the Hog1 mitogen-activated protein kinase (MAPK), which regulates diverse osmoadaptive responses. Hkr1 is a large, highly glycosylated, single-path transmembrane protein that is a putative osmosensor in one of the Hog1 upstream pathways termed the HKR1 subbranch. The extracellular region of Hkr1 contains both a positive and a negative regulatory domain. However, the function of the cytoplasmic domain of Hkr1 (Hkr1-cyto) is unknown. Here, using a mass spectrometric method, we identified a protein, termed Ahk1 (Associated with Hkr1), that binds to Hkr1-cyto. Deletion of the AHK1 gene (in the absence of other Hog1 upstream branches) only partially inhibited osmostress-induced Hog1 activation. In contrast, Hog1 could not be activated by constitutively active mutants of the Hog1 pathway signaling molecules Opy2 or Ste50 in ahk1Δ cells, whereas robust Hog1 activation occurred in AHK1(+) cells. In addition to Hkr1-cyto binding, Ahk1 also bound to other signaling molecules in the HKR1 subbranch, including Sho1, Ste11, and Pbs2. Although osmotic stimulation of Hkr1 does not activate the Kss1 MAPK, deletion of AHK1 allowed Hkr1 to activate Kss1 by cross talk. Thus, Ahk1 is a scaffold protein in the HKR1 subbranch and prevents incorrect signal flow from Hkr1 to Kss1.

Indexed as

Signal TransductionCarrier ProteinsCytoplasmMAP Kinase Kinase KinasesMembrane ProteinsMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesNuclear Matrix-Associated ProteinsOsmoregulationOsmotic PressureProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAhk1 protein, S cerevisiaeCarrier ProteinsHKR1 protein, S cerevisiaeKSS1 protein, S cerevisiaeMAP Kinase Kinase KinasesMembrane ProteinsMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesNuclear Matrix-Associated ProteinsPBS2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSHO1 protein, S cerevisiaeSte11 protein, S cerevisiae

Identifiers

PMID26787842
PMCPMC4800789
OpenAlexW2323487305

What OpenQuestion holds

Textmetadata
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Registered trials

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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.