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. 1988 Nov;85(22):8747–8750. doi: 10.1073/pnas.85.22.8747

Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium.

S Supattapone 1, S K Danoff 1, A Theibert 1, S K Joseph 1, J Steiner 1, S H Snyder 1
PMCID: PMC282538  PMID: 2847175

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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