Evidence map›Paper›PMID 11985722›Full record

ArticleMolecular microbiology2002

A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1.

Wei Tao, Cheryl L Malone, Addison D Ault, Robert J Deschenes, Jan S Fassler

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

28 citing papers in PubMed, 55 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Wei TaoDepartment of Biological Sciences, University of Iowa, Iowa City 52242, USA.
Cheryl L Malone
Addison D Ault
Robert J Deschenes
Jan S Fassler
University of Iowa · US

Funding

SIGNAL TRANSDUCTION BY A YEAST TWO COMPONENT REGULATORR01GM056719 · NIGMS · UNIVERSITY OF IOWA · PI FASSLER, JAN S. · 1998 to 2005
$1.7M
Regulation of eukaryotic histidine kinasesR01GM068746 · NIGMS · UNIVERSITY OF IOWA · PI DESCHENES, ROBERT J · 2003 to 2006
$1.1M
NIA NIH HHS T32AGNIGMS NIH HHS GM56719NIGMS NIH HHS R01 GM056719NIGMS NIH HHS R01 GM068746
6 · The paper itself

Abstract

The yeast histidine kinase, Sln1p, is a plasma membrane-associated osmosensor that regulates the activity of the osmotic stress MAP kinase pathway. Changes in the osmotic environment of the cell influence the autokinase activity of the cytoplasmic kinase domain of Sln1p. Neither the nature of the stimulus, the mechanism by which the osmotic signal is transduced nor the manner in which the kinase is regulated is currently clear. We have identified several mutations located in the linker region of the Sln1 kinase (just upstream of the kinase domain) that cause hyperactivity of the Sln1 kinase. This region of histidine kinases is largely uncharacterized, but its location between the transmembrane domains and the cytoplasmic kinase domain suggests that it may have a potential role in signal transduction. In this study, we have investigated the Sln1 linker region in order to understand its function in signal transduction and regulation of Sln1 kinase activity. Our results indicate that the linker region forms a coiled-coil structure and suggest a mechanism by which alterations induced by osmotic stress influence kinase activity by altering the alignment of the phospho-accepting histidine with respect to the catalytic domain of the kinase.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBinding SitesCCAAT-Enhancer-Binding ProteinsCytoplasmFungal ProteinsIntracellular Signaling Peptides and ProteinsLeucine ZippersMolecular Sequence DataMutagenesisPhenotypeProtein KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeStructure-Activity RelationshipCCAAT-Enhancer-Binding ProteinsFungal ProteinsIntracellular Signaling Peptides and ProteinsProtein KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSLN1 protein, S cerevisiae

Identifiers

PMID11985722
PMCPMC2892222
OpenAlexW1818179740

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.