ArticleNucleic acids research2016
The Hsp70 homolog Ssb and the 14-3-3 protein Bmh1 jointly regulate transcription of glucose repressed genes in Saccharomyces cerevisiae.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
- Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2.Cellular and molecular life sciences : CMLS · 2026Article
- Adh1-Programmed SNF1 Phosphogradients Decrypt Morphogenesis in Candida albicans: Chemical Interrogation Unveils Hyphal Transition Thresholds.Microbial biotechnology · 2026Article
- InAIMS microbiology · 2025Article
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- The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.Frontiers in molecular biosciences · 2024Review
- [NKD1 promotes glucose uptake in colon cancer cells by activating YWHAE transcription].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023Article
- HEAT SHOCK PROTEIN 90.6 interacts with carbon and nitrogen metabolism components during seed development.Plant physiology · 2023Article
- Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022Article
- Article
- Sugar starvation-regulated MYBS2 and 14-3-3 protein interactions enhance plant growth, stress tolerance, and grain weight in rice.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway.Nature communications · 2017Article
- Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.Nature structural & molecular biology · 2017Review
- Article
- The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.Current genetics · 2017Review
- Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.Nature communications · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones of the Hsp70 family interact with a multitude of newly synthesized polypeptides and prevent their aggregation. Saccharomyces cerevisiae cells lacking the Hsp70 homolog Ssb suffer from pleiotropic defects, among others a defect in glucose-repression. The highly conserved heterotrimeric kinase SNF1/AMPK (AMP-activated protein kinase) is required for the release from glucose-repression in yeast and is a key regulator of energy balance also in mammalian cells. When glucose is available the phosphatase Glc7 keeps SNF1 in its inactive, dephosphorylated state. Dephosphorylation depends on Reg1, which mediates targeting of Glc7 to its substrate SNF1. Here we show that the defect in glucose-repression in the absence of Ssb is due to the ability of the chaperone to bridge between the SNF1 and Glc7 complexes. Ssb performs this post-translational function in concert with the 14-3-3 protein Bmh, to which Ssb binds via its very C-terminus. Raising the intracellular concentration of Ssb or Bmh enabled Glc7 to dephosphorylate SNF1 even in the absence of Reg1. By that Ssb and Bmh efficiently suppressed transcriptional deregulation of Δreg1 cells. The findings reveal that Ssb and Bmh comprise a new chaperone module, which is involved in the fine tuning of a phosphorylation-dependent switch between respiration and fermentation.
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