ArticleBiology open2015
E4-Ubiquitin ligase Ufd2 stabilizes Yap8 and modulates arsenic stress responses independent of the U-box motif.
Article in Biology open, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Regulatory Mechanisms Underlying Arsenic Uptake, Transport, and Detoxification in Rice.International journal of molecular sciences · 2023Review
- Adaptation of the yeast gene knockout collection is near-perfectly predicted by fitness and diminishing return epistasis.G3 (Bethesda, Md.) · 2022Article
- Etp1 confers arsenite resistance by affecting ACR3 expression.FEMS yeast research · 2022Article
- Differential Degradation of TRA2A and PYCR2 Mediated by Ubiquitin E3 Ligase E4B.Frontiers in cell and developmental biology · 2022Article
- Yeast AP-1 like transcription factors (Yap) and stress response: a current overview.Microbial cell (Graz, Austria) · 2019Review
- Article
- Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.Frontiers in plant science · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adaptation of Saccharomyces cerevisiae cells to arsenic stress is mediated through the activation of arsenic detoxification machinery by the Yap8 transcription factor. Yap8 is targeted by the ubiquitin proteasome system for degradation under physiological conditions, yet it escapes proteolysis in arsenic-injured cells by a mechanism that remains to be elucidated. Here, we show that Ufd2, an E4-Ubiquitin (Ub) ligase, is upregulated by arsenic compounds both at mRNA and protein levels. Under these conditions, Ufd2 interacts with Yap8 mediating its stabilization, thereby controlling expression of ACR3 and capacity of cells to adapt to arsenic injury. We also show that Ufd2 U-box domain, which is associated to the ubiquitination activity of specific ubiquitin ligases, is dispensable for Yap8 stability and has no role in cell tolerance to arsenic stress. Thus, our data disclose a novel Ufd2 role beyond degradation. This finding is further supported by genetic analyses showing that proteins belonging to Ufd2 proteolytic pathways, namely Ubc4, Rad23 and Dsk2, mediate Yap8 degradation.
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