Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae

Simona Panni, Christiane Landgraf, Rudolf Volkmer-Engert, Gianni Cesareni, Luisa Castagnoli

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)53-63
Number of pages11
JournalFEMS Yeast Research
Volume8
Issue number1
DOIs
Publication statusPublished - Feb 2008

Keywords

  • 14-3-3
  • Bmh1p
  • Bmh2p
  • Nth1p
  • Trehalose

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology
  • Infectious Diseases

Fingerprint Dive into the research topics of 'Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae'. Together they form a unique fingerprint.

  • Cite this