화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.322, No.2, 477-482, 2004
Phosphorylation of teleost phosducins and its effect on the affinity to G-protein beta gamma subunits
Phosducin (PD) is a regulatory protein involved in the phototransduction cascade of vertebrate photoreceptor cells. We have previously demonstrated that there are rod- and cone-specific PDs (O/PD-R and O/PD-C) in the retina of the teleost fish, medaka (Oryzias latipes) [FEBS Lett. 502 (2001) 117]. A 6x His affinity precipitation assay revealed that phosphorylation by either protein kinase A (PKA) or Ca2+/calmodulin-dependent kinase II (CaMKII) reduced the affinity of recombinant medaka PDs to endogenous medaka G-protein beta gamma subunits (Gbetagamma). These results suggest that the affinity of medaka PDs to Gbeta7 is regulated by cAMP and Ca2+ concentrations as also found for mammalian PDs. However, we found a specific difference in the phosphorylation patterns between recombinant O/PD-R and O/PD-C, which resulted in different affinities to Gbetagamma. These differences may affect the light/dark-adaptation between medaka rods and cones. (C) 2004 Elsevier Inc. All rights reserved.