Evidence map›Paper›PMID 26598606›Full record

ArticleMolecular and cellular biology2016

Binding of the Extracellular Eight-Cysteine Motif of Opy2 to the Putative Osmosensor Msb2 Is Essential for Activation of the Yeast High-Osmolarity Glycerol Pathway.

Katsuyoshi Yamamoto, Kazuo Tatebayashi, Haruo Saito

Abstract 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 15 papers.

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0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
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  13. Stress Adaptation.Microbiology spectrum · 2017
    Review
  14. Review
  15. 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

3 authors.

Katsuyoshi YamamotoDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan.
Kazuo TatebayashiDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan tategone@ims.u-tokyo.ac.jp h-saito@ims.u-tokyo.ac.jp.
Haruo SaitoDivision of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan tategone@ims.u-tokyo.ac.jp h-saito@ims.u-tokyo.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To adapt to environmental high osmolarity, the budding yeast Saccharomyces cerevisiae activates the Hog1 mitogen-activated protein kinase, which regulates diverse osmoadaptive responses. Hog1 is activated through the high-osmolarity glycerol (HOG) pathway, which consists of independent upstream signaling routes termed the SLN1 branch and the SHO1 branch. Here, we report that the extracellular cysteine-rich (CR) domain of the transmembrane-anchor protein Opy2 binds to the Hkr1-Msb2 homology (HMH) domain of the putative osmosensor Msb2 and that formation of the Opy2-Msb2 complex is essential for osmotic activation of Hog1 through the MSB2 subbranch of the SHO1 branch. By analyzing the phenotypes of mutants with Opy2 cysteine-to-alanine mutations, we deduced that the CR domain forms four intramolecular disulfide bonds. To probe for the potential induction of conformational changes in the Opy2-Msb2 complex by osmostress, we constructed mutants with a site-specific Cys-to-Ala mutation of the Opy2 CR domain and mutants with a Cys substitution of the Msb2 HMH domain. Each of these mutants had a reduced cysteine. These mutants were then combinatorially cross-linked using chemical cross-linkers of different lengths. Cross-linking between Opy2 Cys48 and Msb2 Cys1023 was sensitive to osmotic changes, suggesting that osmostress induced a conformational change. We therefore propose that the Opy2-Msb2 complex might serve as an osmosensor.

Indexed as

Amino Acid SequenceCysteineGlycerolIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitogen-Activated Protein KinasesMolecular Sequence DataOsmotic PressureProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSignal TransductionCysteineGlycerolHOG1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitogen-Activated Protein KinasesMSB2 protein, S cerevisiaeOpy2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID26598606
PMCPMC4719420

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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.