Evidence map›Paper›PMID 12944490›Full record

ArticleMolecular and cellular biology2003

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

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

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

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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

4 authors.

Naoto SatoInstitute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
Hiroyuki Kawahara
Akio Toh-e
Tatsuya Maeda

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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) kinase kinase kinase, which in turn activates the downstream components of the high-osmolarity glycerol response (HOG) MAP kinase cascade. Here, we report a novel inactivation mechanism for Ssk1p involving degradation by the ubiquitin-proteasome system. Degradation is regulated by the phosphotransfer from Ypd1p to Ssk1p, insofar as unphosphorylated Ssk1p is degraded more rapidly than phosphorylated Ssk1p. Ubc7p/Qri8p, an endoplasmic reticulum-associated ubiquitin-conjugating enzyme, is involved in the phosphorelay-regulated degradation of Ssk1p. In ubc7Delta cells in which the degradation is hampered, the dephosphorylation and/or inactivation process of the Hog1p MAP kinase is delayed compared with wild-type cells after the hyperosmotic treatment. Our results indicate that unphosphorylated Ssk1p is selectively degraded by the Ubc7p-dependent ubiquitin-proteasome system and that this mechanism downregulates the HOG pathway after the completion of the osmotic adaptation.

Indexed as

Ubiquitin-Conjugating EnzymesBiological TransportCysteine EndopeptidasesDNA-Binding ProteinsDown-RegulationIntracellular Signaling Peptides and ProteinsLigasesMAP Kinase Kinase KinasesMAP Kinase Signaling SystemMultienzyme ComplexesMutationOsmosisPhosphorylationProteasome Endopeptidase ComplexProtein KinasesProtein Serine-Threonine KinasesCysteine EndopeptidasesDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsLigasesMAP Kinase Kinase KinasesMultienzyme ComplexesProteasome Endopeptidase ComplexProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSKN7 protein, S cerevisiaeSSK1 protein, S cerevisiaeSSK2 protein, S cerevisiaeTranscription FactorsUBC7 protein, S cerevisiaeUbiquitinUbiquitin-Conjugating EnzymesYPD1 protein, S cerevisiae

Identifiers

PMID12944490
PMCPMC193698

What OpenQuestion holds

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Read underepoch 390

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.