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

doi:10.1016/S0006-291X(05)81219-7

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

124 Scopus citations

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 language	English (US)
Pages (from-to)	192-198
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	175
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(05)81219-7
State	Published - Feb 28 1991

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(05)81219-7

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

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.",

author = "Ferris, {Christopher D.} and Cameron, {Andrew M.} and Bredt, {David S.} and Huganir, {Richard L.} and Snyder, {Solomon H.}",

note = "Funding Information: The authors with to thank Dr. Shengabamurthi for expert assistance in sequencing the peptides. Supported by USPHS grants MH-18501, Research Scientist Award DA-00074 to SHS, predoctoral fellowship MH-10018 to CDF, training grant GM-07309 to DSB and a gift from Bristol-Myers Squibb.",

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T1 - Inositol 1,4,5-trisphosphate receptor is phosphorylated by cyclic AMP-dependent protein kinase at serines 1755 and 1589

AU - Ferris, Christopher D.

AU - Cameron, Andrew M.

AU - Bredt, David S.

AU - Huganir, Richard L.

AU - Snyder, Solomon H.

N1 - Funding Information: The authors with to thank Dr. Shengabamurthi for expert assistance in sequencing the peptides. Supported by USPHS grants MH-18501, Research Scientist Award DA-00074 to SHS, predoctoral fellowship MH-10018 to CDF, training grant GM-07309 to DSB and a gift from Bristol-Myers Squibb.

PY - 1991/2/28

Y1 - 1991/2/28

N2 - 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.

AB - 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.

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

Abstract

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