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Article

Phosphorelay-regulated degradation of the yeast Ssk1p response regulator by the ubiquitin-proteasome system.

Molecular and cellular biology - 1 Sept 2003

Sato Naoto, Kawahara Hiroyuki, Toh-e Akio, Maeda Tatsuya

Abstract excerpt

In Saccharomyces cerevisiae, a phosphorelay signal transduction pathway composed of Sln1p, Ypd1p, and Ssk1p, which are homologous to bacterial two-component signal transducers, is involved in the osmosensing mechanism. In response to high osmolarity, the phosphorelay system is inactivated and Ssk1p remains unphosphorylated. Unphosphorylated Ssk1p binds to and activates the Ssk2p mitogen-activated protein (MAP)...

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Identifiers

PMID: 12944490
DOI: 10.1128/MCB.23.18.6662-6671.2003
PMCID: PMC193698

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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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Phosphorelay-regulated degradation of the yeast Ssk1p response regulator by the ubiquitin-proteasome system.PMID 12944490Read ↗

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Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator.Semantic proximity Read ↗

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Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor.Semantic proximity Read ↗

Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase.Semantic proximity Read ↗

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