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 language | English |
|---|---|
| Pages (from-to) | 53-63 |
| Number of pages | 11 |
| Journal | FEMS Yeast Research |
| Volume | 8 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Feb 2008 |
Fingerprint
Keywords
- 14-3-3
- Bmh1p
- Bmh2p
- Nth1p
- Trehalose
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Microbiology
- Infectious Diseases
Cite this
Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae. / Panni, Simona; Landgraf, Christiane; Volkmer-Engert, Rudolf; Cesareni, Gianni; Castagnoli, Luisa.
In: FEMS Yeast Research, Vol. 8, No. 1, 02.2008, p. 53-63.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae
AU - Panni, Simona
AU - Landgraf, Christiane
AU - Volkmer-Engert, Rudolf
AU - Cesareni, Gianni
AU - Castagnoli, Luisa
PY - 2008/2
Y1 - 2008/2
N2 - 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.
AB - 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.
KW - 14-3-3
KW - Bmh1p
KW - Bmh2p
KW - Nth1p
KW - Trehalose
UR - http://www.scopus.com/inward/record.url?scp=38349132555&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=38349132555&partnerID=8YFLogxK
U2 - 10.1111/j.1567-1364.2007.00312.x
DO - 10.1111/j.1567-1364.2007.00312.x
M3 - Article
VL - 8
SP - 53
EP - 63
JO - FEMS Yeast Research
JF - FEMS Yeast Research
SN - 1567-1356
IS - 1
ER -