Journal
BIOPHYSICAL JOURNAL
Volume 103, Issue 9, Pages 1960-1969Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2012.09.021
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Funding
- Czech Science Foundation [P305/11/0708]
- Grant Agency of Charles University in Prague [28510]
- Ministry of Education, Youth, and Sports of the Czech Republic Research [MSM0021620857]
- Academy of Sciences of the Czech Republic [RVO 67985823]
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Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural changes of Pdc induced by phosphorylation and 14-3-3 protein binding using time-resolved fluorescence spectroscopy. Our data show that the phosphorylation of the N-terminal domain of Pdc at Ser-54 and Ser-73 affects the structure of the whole Pdc molecule. Complex formation with 14-3-3 reduces the flexibility of both the N- and C-terminal domains of phosphorylated Pdc, as determined by time-resolved tryptophan and dansyl fluorescence. Therefore, our data suggest that phosphorylated Pdc undergoes a conformational change when binding to 14-3-3. These changes involve the G(t)beta gamma binding surface within the N-terminal domain of Pdc, and thus could explain the inhibitory effect of 14-3-3 on Pdc function.
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