ArticleMolecular and cellular biology2010
14-3-3 (Bmh) proteins inhibit transcription activation by Adr1 through direct binding to its regulatory domain.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.Frontiers in molecular biosciences · 2024Review
- Molecular association ofFrontiers in cellular and infection microbiology · 2023Review
- Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021Review
- Article
- Bioinformatic analysis reveals new determinants of antigenic 14-3-3 proteins and a novel antifungal strategy.PloS one · 2017Article
- Less is more: Nutrient limitation induces cross-talk of nutrient sensing pathways with NADFrontiers in biology · 2015Article
- Molecular mechanism of flocculation self-recognition in yeast and its role in mating and survival.mBio · 2015Article
- Yeast 14-3-3 protein functions as a comodulator of transcription by inhibiting coactivator functions.The Journal of biological chemistry · 2014Article
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
- Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif.Eukaryotic cell · 2014Article
- 14-3-3 (Bmh) proteins regulate combinatorial transcription following RNA polymerase II recruitment by binding at Adr1-dependent promoters in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
- Nutritional control of growth and development in yeast.Genetics · 2012Review
- The AMP-activated protein kinase Snf1 regulates transcription factor binding, RNA polymerase II activity, and mRNA stability of glucose-repressed genes in Saccharomyces cerevisiae.The Journal of biological chemistry · 2012Article
- Pichia pastoris 14-3-3 regulates transcriptional activity of the methanol inducible transcription factor Mxr1 by direct interaction.Molecular microbiology · 2012Article
- Genetic screening for regulators of Prz1, a transcriptional factor acting downstream of calcineurin in fission yeast.The Journal of biological chemistry · 2012Article
- Review
- Activator-independent transcription of Snf1-dependent genes in mutants lacking histone tails.Molecular microbiology · 2011Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
14-3-3 proteins, known as Bmh in yeast, are ubiquitous, highly conserved proteins that function as adaptors in signal transduction pathways by binding to phosphorylated proteins to activate, inactivate, or sequester their substrates. Bmh proteins have an important role in glucose repression by binding to Reg1, the regulatory subunit of Glc7, a protein phosphatase that inactivates the AMP-activated protein kinase Snf1. We describe here another role for Bmh in glucose repression. We show that Bmh binds to the Snf1-dependent transcription factor Adr1 and inhibits its transcriptional activity. Bmh binds within the regulatory domain of Adr1 between amino acids 215 and 260, the location of mutant ADR1(c) alleles that deregulate Adr1 activity. This provides the first explanation for the phenotype resulting from these mutations. Bmh inhibits Gal4-Adr1 fusion protein activity by binding to the Ser230 region and blocking the function of a nearby cryptic activating region. ADR1(c) alleles, or the inactivation of Bmh, relieve the inhibition and Snf1 dependence of this activating region, indicating that the phosphorylation of Ser230 and Bmh are important for the inactivation of Gal4-Adr1. The Bmh binding domain is conserved in orthologs of Adr1, suggesting that it acquired an important biological function before the whole-genome duplication of the ancestor of S. cerevisiae.
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