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  • Title: Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae.
    Author: Panni S, Landgraf C, Volkmer-Engert R, Cesareni G, Castagnoli L.
    Journal: FEMS Yeast Res; 2008 Feb; 8(1):53-63. PubMed ID: 17916074.
    Abstract:
    In higher eukaryotes, 14-3-3 proteins participate in numerous cellular processes, and carry out their function through a variety of different molecular mechanisms, including regulation of protein localization and enzyme activation. Here, it is shown that the two yeast 14-3-3 homologues, Bmh1p and Bmh2p, form a complex with neutral trehalase (Nth1p), an enzyme that is responsible for trehalose degradation and is required in a variety of stress conditions. In a purified in vitro system, either one of the two 14-3-3 yeast isoforms are necessary for complete activation of neutral trehalase (Nth1p) after phosphorylation by PKA. It is further demonstrated that Bmh1p and Bmh2p bind to the amino-terminal region of phosphorylated trehalase, thereby modulating its enzymatic activity. This work represents the first demonstration of enzyme activation mediated by 14-3-3 binding in yeast.
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