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

S. Supattapone, S. K. Danoff, A. Theibert, S. K. Joseph, J. Steiner, S. H. Snyder

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)8747-8750
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number22
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium'. Together they form a unique fingerprint.

Cite this