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Role of the 14-3-3 protein in the regulation of phosducin function

Description: 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.
Amount: CZK 6,340,000
Funding type: grant
Funder scheme: Standard Projects
Start date: 2011-01-01
End date: 2015-12-31
Institutions: Charles University, Univerzita Karlova
Funded outputs count: 5
Funder award ID: GAP305/11/0708
OpenAlex ID: G5582529068
2013 · Petr Vacha, Iva Zuskova, et al. · Biophysical Chemistry · 12
2012 · Lenka Rezabkova, Miroslava Kacirova, et al. · Biophysical Journal · 14
2010 · Tomas Obsil, Veronika Obsilova · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · 113
2009 · M. Anuradha, K. N. Rao, et al. · Indian Journal of Plant Physiology · 1