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Cited by 352

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

Open access
Supattapone, S, Danoff, S K, Theibert, A, Joseph, S K, Steiner, J, Snyder, S H·1988·Proceedings of the National Academy of Sciences

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.

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Metadata

Authors
Supattapone, S., Danoff, S. K., Theibert, A., Joseph, S. K., Steiner, J., & Snyder, S. H.
Venue
Proceedings of the National Academy of Sciences
Published
1988-11
Volume
85
Issue
22
Pages
8747-8750
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2021094409
Cited by
352
References
0
FWCI
8.51
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium. https://app.cochat.ai/papers/10.1073/pnas.85.22.8747
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Supattapone, S., Danoff, S. K., Theibert, A., Joseph, S. K., Steiner, J., & Snyder, S. H. (1988). Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.85.22.8747

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.