ArticleThe Journal of biological chemistry2012
Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Oxidative stress-responsive cell wall remodeling depends on phosphate in Candida albicans.Nature communications · 2026Article
- Integrative Epigenetic and Molecular Analysis Reveals a Novel Promoter for a New Isoform of the Transcription Factor TEAD4.International journal of molecular sciences · 2024Article
- Halofantrine Hydrochloride Acts as an Antioxidant Ability Inhibitor That Enhances Oxidative Stress Damage toAntioxidants (Basel, Switzerland) · 2024Article
- Roles of the CCR4-Not complex in translation and dynamics of co-translation events.Wiley interdisciplinary reviews. RNA · 2023Review
- Cytoplasmic YAP1-mediated ESCRT-III assembly promotes autophagic cell death and is ubiquitinated by NEDD4L in breast cancer.Cancer communications (London, England) · 2023Article
- The APC/C Activator Cdh1p Plays a Role in Mitochondrial Metabolic Remodelling in Yeast.International journal of molecular sciences · 2023Article
- VOZ1 and VOZ2 transcription factors regulate arsenic tolerance and distribution in rice and Arabidopsis.Frontiers in plant science · 2023Article
- Manganese Stress Tolerance Depends on Yap1 and Stress-Activated MAP Kinases.International journal of molecular sciences · 2022Article
- Ccr4-Not as a mediator of environmental signaling: a jack of all trades and master of all.Current genetics · 2021Review
- The C-terminal region of yeast ubiquitin-protein ligase Not4 mediates its cellular localization and stress response.FEMS microbiology letters · 2021Article
- The CNOT4 Subunit of the CCR4-NOT Complex is Involved in mRNA Degradation, Efficient DNA Damage Repair, and XY Chromosome Crossover during Male Germ Cell Meiosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Review
- Identification of ubiquitin-proteasome system components affecting the degradation of the transcription factor Pap1.Redox biology · 2020Article
- Ccr4-Not maintains genomic integrity by controlling the ubiquitylation and degradation of arrested RNAPII.Genes & development · 2019Article
- The molecular biology of fruity and floral aromas in beer and other alcoholic beverages.FEMS microbiology reviews · 2019Review
- A conserved CAF40-binding motif in metazoan NOT4 mediates association with the CCR4-NOT complex.Genes & development · 2019Article
- The conserved RNA recognition motif and C3H1 domain of the Not4 ubiquitin ligase regulate in vivo ligase function.Scientific reports · 2018Article
- Inhibition of YAP function overcomes BRAF inhibitor resistance in melanoma cancer stem cells.Oncotarget · 2017Article
- Mutations in theFrontiers in genetics · 2017Article
- DNA replication inhibitor hydroxyurea alters Fe-S centers by producing reactive oxygen species in vivo.Scientific reports · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
Saccharomyces cerevisiae Yap1 is a transcriptional regulatory protein that serves as a central determinant of oxidative stress tolerance. Activity of this factor is regulated in large part by control of its subcellular location. In the absence of oxidants, Yap1 is primarily located in the cytoplasm. Upon oxidant challenge, Yap1 accumulates rapidly in the nucleus where it activates expression of genes required for oxidative stress tolerance such as the thioredoxin TRX2. Here, we demonstrate that Yap1 degradation is accelerated in response to oxidative stress. Yap1 is folded differently depending on the oxidant used to induce its nuclear localization but is degraded similarly, irrespective of its folded status. Mutant forms of Yap1 that are constitutively trapped in the nucleus are degraded in the absence of an oxidant signal. Degradation requires the ability of the protein to bind DNA and a domain in the amino-terminal region of the factor. Inhibition of the proteasome prevents Yap1 turnover. Screening a variety of mutants involved in ubiquitin-mediated proteolysis demonstrated an important role for the nuclear ubiquitin ligase Not4 in Yap1 degradation. Not4 was found to bind to Yap1 in an oxidant-stimulated fashion. The Candida albicans Yap1 homologue (Cap1) also was degraded after oxidant challenge. These data uncover a new, conserved pathway for regulation of the oxidative stress response that serves to temporally limit the duration of Yap1-dependent transcriptional activation.
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