Open AccessCyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium.
Author(s) -
Surachai Supattapone,
Sonye K. Danoff,
Anne B. Theibert,
Suresh K. Joseph,
Joseph P. Steiner,
Solomon H. Snyder
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.22.8747
Subject(s) - inositol , inositol trisphosphate , second messenger system , phosphorylation , inositol trisphosphate receptor , protein kinase a , protein phosphorylation , biochemistry , inositol phosphate , gq alpha subunit , calmodulin , biology , calcium , chemistry , microbiology and biotechnology , receptor , g protein , enzyme , organic chemistry
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.