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PMID: 1848697 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Inositol trisphosphate receptor: phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 6 ·1991-03-15 ·Pages 2232-5

Ferris CD, Huganir RL, Bredt DS, Cameron AM, Snyder SH

Abstract

We have previously demonstrated that the inositol 1,4,5-trisphosphate (IP3) receptor is phosphorylated by cyclic AMP-dependent protein kinase (PKA). In the present study, phosphorylation of IP3 receptors has been examined with purified receptor protein reconstituted in liposomes to remove detergent that can inhibit protein kinases. The IP3 receptor is stoichiometrically phosphorylated by protein kinase C (PKC) and Ca2+ calmodulin-dependent protein kinase II (CaM kinase II) as well as by PKA. Phosphorylation by the three enzymes is additive and involves different peptide sequences. Phosphorylation by PKC, which is stimulated by Ca2+ and diacylglycerol, and by CaM kinase II, which requires Ca2+, provides means whereby Ca2+ and diacylglycerol, formed during inositol phospholipid turnover, may regulate IP3 receptor physiology.

MeSH Terms

Calcium Channels Calcium-Calmodulin-Dependent Protein Kinases Inositol 1,4,5-Trisphosphate/metabolism Inositol 1,4,5-Trisphosphate Receptors Kinetics Liposomes Peptide Mapping Phosphopeptides/isolation & purification Phosphorylation Protein Kinase C/metabolism Protein Kinases/metabolism Proteolipids/metabolism Receptors, Cell Surface/metabolism Receptors, Cytoplasmic and Nuclear

Chemicals

Calcium Channels Inositol 1,4,5-Trisphosphate Receptors Liposomes Phosphopeptides Proteolipids Receptors, Cell Surface Receptors, Cytoplasmic and Nuclear proteoliposomes Inositol 1,4,5-Trisphosphate Protein Kinases Protein Kinase C Calcium-Calmodulin-Dependent Protein Kinases

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Ferris C D

Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Huganir R L

Bredt D S

Cameron A M

Snyder S H

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.88.6.2232

Published

1991-03-15

Pages

2232-5

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC51204

Subset

Grants

NIDA NIH HHS · DA-00074 · United States

NIGMS NIH HHS · GM-07309 · United States

NIMH NIH HHS · MH-18501 · United States

External Links

PubMed source DOI: 10.1073/pnas.88.6.2232 PMC Full Text View journal details

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Inositol trisphosphate receptor: phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles.

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