ArticleProceedings of the National Academy of Sciences of the United States of America2017
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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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32 citing papers in PubMed, 72 citations in OpenAlex.
- Bifunctional trehalase FsTreA coordinates intracellular mobilization and extracellular utilization of trehalose to modulate virulence inApplied and environmental microbiology · 2026Article
- Structural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16.Nature communications · 2026Article
- Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026Article
- A trehalase-derived MAMP triggers LecRK-V-mediated immune responses inScience advances · 2025Article
- Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8.The Journal of biological chemistry · 2025Review
- Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins.Physiological research · 2024Review
- 14-3-3 Protein-Protein Interactions: From Mechanistic Understanding to Their Small-Molecule Stabilization.Chembiochem : a European journal of chemical biology · 2024Review
- Rapamycin-sensitive mechanisms confine the growth of fission yeast below the temperatures detrimental to cell physiology.iScience · 2024Article
- The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.Frontiers in molecular biosciences · 2024Review
- 14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices.Protein science : a publication of the Protein Society · 2023Article
- Human 14-3-3 Proteins Site-selectively Bind the Mutational Hotspot Region of SARS-CoV-2 Nucleoprotein Modulating its Phosphoregulation.Journal of molecular biology · 2023Article
- Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.Journal of structural biology · 2022Article
- Crystal structure of potato 14-3-3 protein St14f revealed the importance of helix I in StFDL1 recognition.Scientific reports · 2022Article
- 14-3-3 Proteins are Potential Regulators of Liquid-Liquid Phase Separation.Cell biochemistry and biophysics · 2022Review
- Genetic screen for suppression of transcriptional interference reveals fission yeast 14-3-3 protein Rad24 as an antagonist of precocious Pol2 transcription termination.Nucleic acids research · 2022Article
- Structural insights into the functional roles of 14-3-3 proteins.Frontiers in molecular biosciences · 2022Review
- Novel acid trehalase belonging to glycoside hydrolase family 37 fromMycoscience · 2022Article
- Identifying carbohydrate-active enzymes of Cutaneotrichosporon oleaginosus using systems biology.Microbial cell factories · 2021Article
- A Structural Study of the Cytoplasmic Chaperone Effect of 14-3-3 Proteins on Ataxin-1.Journal of molecular biology · 2021Article
- 14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites.Communications biology · 2021Article
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7 authors at 2 institutions in 1 country.
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Abstract
The 14-3-3 proteins, a family of highly conserved scaffolding proteins ubiquitously expressed in all eukaryotic cells, interact with and regulate the function of several hundreds of partner proteins. Yeast neutral trehalases (Nth), enzymes responsible for the hydrolysis of trehalose to glucose, compared with trehalases from other organisms, possess distinct structure and regulation involving phosphorylation at multiple sites followed by binding to the 14-3-3 protein. Here we report the crystal structures of yeast Nth1 and its complex with Bmh1 (yeast 14-3-3 isoform), which, together with mutational and fluorescence studies, indicate that the binding of Nth1 by 14-3-3 triggers Nth1's activity by enabling the proper 3D configuration of Nth1's catalytic and calcium-binding domains relative to each other, thus stabilizing the flexible part of the active site required for catalysis. The presented structure of the Bmh1:Nth1 complex highlights the ability of 14-3-3 to modulate the structure of a multidomain binding partner and to function as an allosteric effector. Furthermore, comparison of the Bmh1:Nth1 complex structure with those of 14-3-3:serotonin
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