ArticleThe Journal of biological chemistry2016
Nitrogen Starvation-induced Phosphorylation of Ras1 Protein and Its Potential Role in Nutrient Signaling and Stress Response.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Multi-Omics Analysis of Multiple Glucose-Sensing Receptor Systems in Yeast.Biomolecules · 2022Article
- Regulation of Copper Metabolism by Nitrogen Utilization inJournal of fungi (Basel, Switzerland) · 2021Article
- Sho1p Connects Glycolysis to Ras1-cAMP Signaling and Is Required for Microcolony Formation in Candida albicans.mSphere · 2020Article
- Phosphorylation of the Gα protein Gpa2 promotes protein kinase A signaling in yeast.The Journal of biological chemistry · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Ras1 is a small GTPase in the budding yeast Saccharomyces cerevisiae that regulates nutrient signaling. It has been shown that Ras1 undergoes phosphorylation, but the functional consequences and regulation of Ras1 phosphorylation remain unknown. Here we identify Ser-226 as an important residue for Ras1 phosphorylation, as mutating this residue to an alanine drastically diminishes the level of Ras1 phosphorylation. Notably, phosphorylated Ras1 accumulates as the cells approach the stationary phase of growth. Likewise, subjecting cells to nitrogen starvation also elevates the level of Ras1 phosphorylation. Interestingly, blocking Ras1 phosphorylation diminishes the level of autophagy and also renders the cells more sensitive to heat shock. Together, these data suggest a role of Ras1 phosphorylation in modulating nutrient signaling and stress response.
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