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

Surachai Supattapone | Zendy; Sonye K. Danoff | Zendy; Anne B. Theibert | Zendy; Suresh K. Joseph | Zendy; J. Steiner | Zendy; S H Snyder | Zendy

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Cyclic 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,

J. Steiner,

S H Snyder

Publication year - 1988

Publication title -

proceedings of the national academy of sciences

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.

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