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Article

Identifying protein kinase-specific effectors of the osmostress response in yeast.

Science signaling - 7 Mar 2017

Romanov Natalie, Hollenstein David Maria, Janschitz Marion, Ammerer Gustav, Anrather Dorothea, Reiter Wolfgang

Abstract excerpt

The budding yeast Saccharomyces cerevisiae reacts to increased external osmolarity by modifying many cellular processes. Adaptive signaling relies primarily on the high-osmolarity glycerol (HOG) pathway, which is closely related to the mammalian p38 mitogen-activated protein kinase (MAPK) pathway in core architecture. To identify target proteins of the MAPK Hog1, we designed a mass spectrometry-based...

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Identifiers

PMID: 28270554
DOI: 10.1126/scisignal.aag2435
PMCID: PMC6049618

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Identifying protein kinase-specific effectors of the osmostress response in yeast.PMID 28270554Read ↗

Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1.Semantic proximity Read ↗

Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress.Semantic proximity Read ↗

An integrated view on a eukaryotic osmoregulation system.Semantic proximity Read ↗

Unique and redundant roles for HOG MAPK pathway components as revealed by whole-genome expression analysis.Semantic proximity Read ↗

MAPK Hog1 closes the S. cerevisiae glycerol channel Fps1 by phosphorylating and displacing its positive regulators.Semantic proximity Read ↗

Crosstalk between Saccharomycescerevisiae SAPKs Hog1 and Mpk1 is mediated by glycerol accumulation.Semantic proximity Read ↗

Surprising regulatory plasticity for the conserved HOG pathway in diverse <i>Saccharomyces cerevisiae</i> strainsSemantic proximity Read ↗

Activation of the Saccharomyces cerevisiae filamentation/invasion pathway by osmotic stress in high-osmolarity glycogen pathway mutants.Semantic proximity Read ↗

Hog1 activation delays mitotic exit via phosphorylation of Net1.Semantic proximity Read ↗

Osmostress induces autophosphorylation of Hog1 via a C-terminal regulatory region that is conserved in p38α.Semantic proximity Read ↗

Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway.Semantic proximity Read ↗

Sphingolipids regulate the yeast high-osmolarity glycerol response pathway.Semantic proximity Read ↗

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