ArticleThe Journal of biological chemistry2013
Ras protein/cAMP-dependent protein kinase signaling is negatively regulated by a deubiquitinating enzyme, Ubp3, in yeast.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Unveiling genetic anchors in saccharomyces cerevisiae: QTL mapping identifies IRA2 as a key player in ethanol tolerance and beyond.Molecular genetics and genomics : MGG · 2024Article
- Deubiquitinase Ubp3 regulates ribophagy and deubiquitinates Smo1 for appressorium-mediated infection by Magnaporthe oryzae.Molecular plant pathology · 2022Article
- Phenomic screen identifies a role for the yeast lysine acetyltransferase NuA4 in the control of Bcy1 subcellular localization, glycogen biosynthesis, and mitochondrial morphology.PLoS genetics · 2020Article
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- Phosphorylation of the Gα protein Gpa2 promotes protein kinase A signaling in yeast.The Journal of biological chemistry · 2019Article
- A novel connection between the Cell Wall Integrity and the PKA pathways regulates cell wall stress response in yeast.Scientific reports · 2017Article
- Review
- The pleiotropic deubiquitinase Ubp3 confers aneuploidy tolerance.Genes & development · 2016Article
- Nitrogen Starvation-induced Phosphorylation of Ras1 Protein and Its Potential Role in Nutrient Signaling and Stress Response.The Journal of biological chemistry · 2016Article
- The Catalytic Activity of the Ubp3 Deubiquitinating Protease Is Required for Efficient Stress Granule Assembly in Saccharomyces cerevisiae.Molecular and cellular biology · 2016Article
- Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance.The EMBO journal · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ras proteins and cAMP-dependent protein kinase (protein kinase A, PKA) are important components of a nutrient signaling pathway that mediates cellular responses to glucose in yeast. The molecular mechanisms that regulate Ras/PKA-mediated signaling remain to be fully understood. Here, we provide evidence that Ras/PKA signaling is negatively regulated by a deubiquitinating enzyme, Ubp3. Disrupting the activity of Ubp3 leads to hyperactivation of PKA, as evidenced by much enhanced phosphorylation of PKA substrates, decreased accumulation of glycogen, larger cell size, and increased sensitivity to heat shock. Levels of intracellular cAMP and the active forms of Ras proteins are also elevated in the ubp3Δ mutant. Consistent with a possibility that the increased cAMP is responsible for the abnormal signaling behavior of the ubp3Δ mutant, overexpressing PDE2, which encodes a phosphodiesterase that hydrolyzes cAMP, significantly relieves the cell size increase and heat shock sensitivity of the mutant. Further analysis reveals that Ubp3 interacts with a Ras GTPase-accelerating protein, Ira2, and regulates its level of ubiquitination. Together, our data indicate that Ubp3 is a new regulator of the Ras/PKA signaling pathway and suggest that Ubp3 regulates this pathway by controlling the ubiquitination of Ras GTPase-accelerating protein Ira2.
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Registered trials
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.