Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cAMP-dependent protein kinase decreases its calcium release potency, providing a biochemical substrate for second-messenger cross-talk.
Suggests PKA phosphorylation modulates IP3 receptor function; leaves open relevance to intact neurons or in vivo calcium signaling.
We report the stoichiometric phosphorylation of an inositol 1,4,5-trisphosphate receptor-binding protein from rat brain by the cAMP-dependent protein kinase but not by protein kinase C or Ca2+/calmodulin-dependent protein kinase. This phosphorylation event does not markedly alter [3H]inositol 1,4,5-trisphosphate-binding characteristics. However, inositol 1,4,5-trisphosphate is only 10% as potent in releasing 45Ca2+ from phosphorylated, as compared with native, cerebellar microsomes. Phosphorylation of the inositol 1,4,5-trisphosphate-binding protein by the cAMP-dependent protein kinase may provide a biochemical substrate for second-messenger cross talk.
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Supattapone et al. (1988) studied this question.
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