Senior researcher
Role of the 14-3-3 protein in the regulation of phosducin function. The main goal is to study the structural basis for the 14-3-3 protein-dependent regulation of phosducin function. Methods of fluorescence spectroscopy, analytical ultracentrifugation and protein crystallography will be used as principal tools. Phosducin specifically binds with high affinity to Gtβg heterodimer and inhibits its interaction with Gtα or other effectors. Thus phosducin down-regulates the light response in photoreceptors. Phosducin function is regulated through the phosphorylation at Ser54 and Ser73 and the binding to the regulatory 14-3-3 protein. The detailed mechanism of the 14-3-3 protein-dependent inhibition of phosducin function is unknown. We propose to perform structural studies of the 14-3-3/phosducin complex, to identify phosducin regions involved in the interaction with 14-3-3 and thus to mechanistically explain the inhibitory role of 14-3-3 in phosducin regulation. The proposed research will increase our understanding concerning not only the role of the 14-3-3 protein in phosducin regulation (and G protein signaling) but the 14-3-3 protein function in general as well.
2014 prof. Professor, Physical chemistry, Charles University, Prague, Faculty of Science
2007 doc. Associate Professor, Physical chemistry, Charles University, Prague, Faculty of Science
1998 Ph.D. Physical chemistry, Charles University, Prague, Faculty of Science
1998 RNDr. Physical chemistry, Charles University, Prague, Faculty of Science
1995 MSc. Physical chemistry, Charles University, Prague, Faculty of Science
E-mail: tomas.obsil@natur.cuni.cz, tel: 00420221951303, own web site
