Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.17 (CaMKII)
 4,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phototransduction is a canonical G protein-mediated cascade of retinal photoreceptor cells that transforms photons into neural responses. Phosducin (Pd) is a Gbetagamma-binding protein that is highly expressed in photoreceptors. Pd is phosphorylated in dark-adapted retina and is dephosphorylated in response to light. Dephosphorylated Pd binds Gbetagamma with high affinity and inhibits the interaction of Gbetagamma with Galpha or other effectors, whereas phosphorylated Pd does not. These results have led to the hypothesis that Pd down-regulates the light response. Consequently, it is important to understand the mechanisms of regulation of Pd phosphorylation. We have previously shown that phosphorylation of Pd by cAMP-dependent protein kinase moderately inhibits its association with Gbetagamma. In this study, we report that Pd was rapidly phosphorylated by Ca(2+)/calmodulin-dependent kinase II, resulting in 100-fold greater inhibition of Gbetagamma binding than cAMP-dependent protein kinase phosphorylation. Furthermore, Pd phosphorylation by Ca(2+)/calmodulin-dependent kinase II at Ser-54 and Ser-73 led to binding of the phosphoserine-binding protein 14-3-3. Importantly, in vivo decreases in Ca(2+) concentration blocked the interaction of Pd with 14-3-3, indicating that Ca(2+) controls the phosphorylation state of Ser-54 and Ser-73 in vivo. These results are consistent with a role for Pd in Ca(2+)-dependent light adaptation processes in photoreceptor cells and also suggest other possible physiological functions.
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PMID:Modulation of the G protein regulator phosducin by Ca2+/calmodulin-dependent protein kinase II phosphorylation and 14-3-3 protein binding. 1133 Dec 85

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 (OlPD-R and OlPD-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 Ca(2+)/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 Gbetagamma is regulated by cAMP and Ca(2+) concentrations as also found for mammalian PDs. However, we found a specific difference in the phosphorylation patterns between recombinant OlPD-R and OlPD-C, which resulted in different affinities to Gbetagamma. These differences may affect the light/dark-adaptation between medaka rods and cones.
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PMID:Phosphorylation of teleost phosducins and its effect on the affinity to G-protein beta gamma subunits. 1532 55