Evidence map›Paper›PMID 18478233›Full record

ArticleCurrent genetics2008

The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.

Lance Shaner, Patrick A Gibney, Kevin A Morano

Open access · greenAbstract read
In one paragraph

Article in Current genetics, 2008. 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
1.5field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

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  17. Surface architecture of histoplasma capsulatum.Frontiers in microbiology · 2011
    Article
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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

3 authors at 1 institution in 1 country.

Lance ShanerDepartment of Microbiology and Molecular Genetics, University of Texas Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
Patrick A Gibney
Kevin A Morano
The University of Texas Health Science Center at Houston · US

Funding

Hsp110 protein chaperone function in yeastR01GM074696 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MORANO, KEVIN ANTHONY · 2006 to 2015
$2.8M
NIGMS NIH HHS GM 074696NIGMS NIH HHS R01 GM074696
6 · The paper itself

Abstract

Molecular chaperones direct refolding and triage decisions and support signal transduction responses to cytotoxic stress. The eukaryotic chaperone Hsp110 is represented by the SSE1/2 genes in Saccharomyces cerevisiae, which act as nucleotide exchange factors (NEFs) for cognate cytosolic Hsp70 chaperones. In this report, we present evidence that Sse1 is required for signaling through the cell integrity pathway via partnership with Hsp90 and the terminal MAP kinase Slt2. We found that sse1Delta and sti1Delta mutant cells share the typical cell integrity mutant phenotypes of osmoremediated temperature-sensitive growth and sensitivity to cell wall-damaging agents. Sse1 binds to Slt2 in vivo and similar to Hsp90 mutants, Slt2 stability and phosphorylation is not compromised in sse1Delta cells, whereas activation of the downstream transcription factor Rlm1 is abolished. In addition to Rlm1, Slt2 activates the Swi4/Swi6 heterodimer SBF in response to cell wall damage. SSE1 displayed dramatic synthetic phenotypes when disrupted in combination with mutations in SBF and the related Mbp1/Swi6 heterodimer MBF, characterized by severe growth and morphological defects. These defects were reversed by restoration of Hsp70 NEF activity, providing a mechanistic model wherein Sse1 functionally partners with Hsp90 as an Hsp70 NEF to promote client protein maturation and interaction with downstream effectors.

Indexed as

Cell WallFungal ProteinsGenes, FungalHeat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMAP Kinase Signaling SystemMitogen-Activated Protein KinasesModels, BiologicalMorphogenesisMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionFungal ProteinsHeat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMitogen-Activated Protein KinasesSaccharomyces cerevisiae ProteinsSLT2 protein, S cerevisiaeSSA3 protein, S cerevisiaeSSE1 protein, S cerevisiaeSTI1 protein, S cerevisiae

Identifiers

PMID18478233
PMCPMC5635425
OpenAlexW2055993297

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.