ArticleEukaryotic cell2004
Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction.
Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Genetic effects on molecular network states explain complex traits.Molecular systems biology · 2023Article
- Oxidative stress response pathways in fungi.Cellular and molecular life sciences : CMLS · 2022Review
- The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017Review
- Stress Response and Pathogenicity of the Necrotrophic Fungal Pathogen Alternaria alternata.Scientifica · 2012Review
- Genome-wide survey of yeast mutations leading to activation of the yeast cell integrity MAPK pathway: novel insights into diverse MAPK outcomes.BMC genomics · 2011Article
- Association of the Skn7 and Yap1 transcription factors in the Saccharomyces cerevisiae oxidative stress response.Eukaryotic cell · 2011Article
- Fungal Skn7 stress responses and their relationship to virulence.Eukaryotic cell · 2011Review
- Hyperosmotic stress signaling to the nucleus disrupts the Ran gradient and the production of RanGTP.Molecular biology of the cell · 2007Article
- Importin alpha1 is involved in the nuclear localization of Zac1 and the induction of p21WAF1/CIP1 by Zac1.The Biochemical journal · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Yeast Sln1p is an osmotic stress sensor with histidine kinase activity. Modulation of Sln1 kinase activity in response to changes in the osmotic environment regulates the activity of the osmotic response mitogen-activated protein kinase pathway and the activity of the Skn7p transcription factor, both important for adaptation to changing osmotic stress conditions. Many aspects of Sln1 function, such as how kinase activity is regulated to allow a rapid response to the continually changing osmotic environment, are not understood. To gain insight into Sln1p function, we conducted a two-hybrid screen to identify interactors. Mog1p, a protein that interacts with the yeast Ran1 homolog, Gsp1p, was identified in this screen. The interaction with Mog1p was characterized in vitro, and its importance was assessed in vivo. mog1 mutants exhibit defects in SLN1-SKN7 signal transduction and mislocalization of the Skn7p transcription factor. The requirement for Mog1p in normal localization of Skn7p to the nucleus does not fully account for the mog1-related defects in SLN1-SKN7 signal transduction, raising the possibility that Mog1p may play a role in Skn7 binding and activation of osmotic response genes.
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