Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein
نویسندگان
چکیده
منابع مشابه
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
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 ph...
متن کاملRole of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1.
Trehalases are important highly conserved enzymes found in a wide variety of organisms and are responsible for the hydrolysis of trehalose that serves as a carbon and energy source as well as a universal stress protectant. Emerging evidence indicates that the enzymatic activity of the neutral trehalase Nth1 in yeast is enhanced by 14-3-3 protein binding in a phosphorylation-dependent manner thr...
متن کاملRole of the EF-hand-like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1.
Trehalases hydrolyze the non-reducing disaccharide trehalose amassed by cells as a universal protectant and storage carbohydrate. Recently, it has been shown that the activity of neutral trehalase Nth1 from Saccharomyces cerevisiae is mediated by the 14-3-3 protein binding that modulates the structure of both the catalytic domain and the region containing the EF-hand-like motif, whose role in t...
متن کاملInhibition of calcium/calmodulin-dependent protein kinase kinase by protein 14-3-3.
Intracellular calcium concentrations regulate diverse cellular events including cytoskeletal dynamics, gene transcription, and synaptic plasticity. The calcium signal is transduced in part by the calcium/calmodulin-dependent protein kinase (CaMK) cascade that is comprised of CaMK kinase (CaMKK) and its primary downstream substrates, CaMKI and CaMKIV. The CaMK cascade also participates in cross-...
متن کاملPlant metabolism: Enzyme regulation by 14-3-3 proteins
14-3-3 proteins have been found to regulate the plant enzyme nitrate reductase by reversible phosphoserine binding. Plant plasma-membrane H(+)-ATPases, transporters that are activated by the phytotoxin fusicoccin, appear to be regulated in a similar fashion.
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ژورنال
عنوان ژورنال: Physiological Research
سال: 2019
ISSN: 1802-9973,0862-8408
DOI: 10.33549/physiolres.933950