Inositol 1,4,5-trisphosphate receptor is phosphorylated by cyclic AMP-dependent protein kinase at serines 1755 and 1589

Christopher D. Ferris, Andrew M Cameron, David S. Bredt, Richard L Huganir, Solomon H Snyder

Research output: Contribution to journalArticle

Abstract

IP3 activates intracellular calcium release by binding to an intracellular ligand gated calcium permeable channel which has been shown to be regulated by protein kinase A phosphorylation. Two consensus sequences for protein kinase A phosphorylation are predicted by the recently isolated cDNA of the mouse and rat. In the present study we have isolated and sequenced the two peptides in the rat IP3 receptor which are phosphorylated by protein kinase A and demonstrate protein kinase A phosphorylation on S-1755 and S-1589.

Original languageEnglish (US)
Pages (from-to)192-198
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume175
Issue number1
DOIs
StatePublished - Feb 28 1991

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Inositol 1,4,5-Trisphosphate Receptors
Cyclic AMP-Dependent Protein Kinases
Serine
Phosphorylation
Rats
Calcium
Consensus Sequence
Calcium Channels
Complementary DNA
Ligands
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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AU - Cameron, Andrew M

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AU - Huganir, Richard L

AU - Snyder, Solomon H

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