Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Nov;85(22):8747–8750. doi: 10.1073/pnas.85.22.8747

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

S Supattapone 1, S K Danoff 1, A Theibert 1, S K Joseph 1, J Steiner 1, S H Snyder 1
PMCID: PMC282538  PMID: 2847175

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.

Full text

PDF
8747

Images in this article

8748Image
on p.8748
8748Image
on p.8748

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baukal A. J., Guillemette G., Rubin R., Spät A., Catt K. J. Binding sites for inositol trisphosphate in the bovine adrenal cortex. Biochem Biophys Res Commun. 1985 Dec 17;133(2):532–538. doi: 10.1016/0006-291x(85)90939-8. [DOI] [PubMed] [Google Scholar]
  2. Berridge M. J., Irvine R. F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature. 1984 Nov 22;312(5992):315–321. doi: 10.1038/312315a0. [DOI] [PubMed] [Google Scholar]
  3. Danoff S. K., Supattapone S., Snyder S. H. Characterization of a membrane protein from brain mediating the inhibition of inositol 1,4,5-trisphosphate receptor binding by calcium. Biochem J. 1988 Sep 15;254(3):701–705. doi: 10.1042/bj2540701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Guillemette G., Balla T., Baukal A. J., Spät A., Catt K. J. Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues. J Biol Chem. 1987 Jan 25;262(3):1010–1015. [PubMed] [Google Scholar]
  5. Hill T. D., Berggren P. O., Boynton A. L. Heparin inhibits inositol trisphosphate-induced calcium release from permeabilized rat liver cells. Biochem Biophys Res Commun. 1987 Dec 31;149(3):897–901. doi: 10.1016/0006-291x(87)90492-x. [DOI] [PubMed] [Google Scholar]
  6. Hokin L. E. Receptors and phosphoinositide-generated second messengers. Annu Rev Biochem. 1985;54:205–235. doi: 10.1146/annurev.bi.54.070185.001225. [DOI] [PubMed] [Google Scholar]
  7. Katada T., Gilman A. G., Watanabe Y., Bauer S., Jakobs K. H. Protein kinase C phosphorylates the inhibitory guanine-nucleotide-binding regulatory component and apparently suppresses its function in hormonal inhibition of adenylate cyclase. Eur J Biochem. 1985 Sep 2;151(2):431–437. doi: 10.1111/j.1432-1033.1985.tb09120.x. [DOI] [PubMed] [Google Scholar]
  8. Kennedy M. B., Greengard P. Two calcium/calmodulin-dependent protein kinases, which are highly concentrated in brain, phosphorylate protein I at distinct sites. Proc Natl Acad Sci U S A. 1981 Feb;78(2):1293–1297. doi: 10.1073/pnas.78.2.1293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Nishizuka Y. Studies and perspectives of protein kinase C. Science. 1986 Jul 18;233(4761):305–312. doi: 10.1126/science.3014651. [DOI] [PubMed] [Google Scholar]
  11. Nishizuka Y. Turnover of inositol phospholipids and signal transduction. Science. 1984 Sep 21;225(4668):1365–1370. doi: 10.1126/science.6147898. [DOI] [PubMed] [Google Scholar]
  12. Rasmussen H., Barrett P. Q. Calcium messenger system: an integrated view. Physiol Rev. 1984 Jul;64(3):938–984. doi: 10.1152/physrev.1984.64.3.938. [DOI] [PubMed] [Google Scholar]
  13. Spät A., Bradford P. G., McKinney J. S., Rubin R. P., Putney J. W., Jr A saturable receptor for 32P-inositol-1,4,5-triphosphate in hepatocytes and neutrophils. Nature. 1986 Feb 6;319(6053):514–516. doi: 10.1038/319514a0. [DOI] [PubMed] [Google Scholar]
  14. Spät A., Fabiato A., Rubin R. P. Binding of inositol trisphosphate by a liver microsomal fraction. Biochem J. 1986 Feb 1;233(3):929–932. doi: 10.1042/bj2330929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Supattapone S., Worley P. F., Baraban J. M., Snyder S. H. Solubilization, purification, and characterization of an inositol trisphosphate receptor. J Biol Chem. 1988 Jan 25;263(3):1530–1534. [PubMed] [Google Scholar]
  16. Walaas S. I., Nairn A. C., Greengard P. PCPP-260, a Purkinje cell-specific cyclic AMP-regulated membrane phosphoprotein of Mr 260,000. J Neurosci. 1986 Apr;6(4):954–961. doi: 10.1523/JNEUROSCI.06-04-00954.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Williamson J. R., Cooper R. H., Joseph S. K., Thomas A. P. Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver. Am J Physiol. 1985 Mar;248(3 Pt 1):C203–C216. doi: 10.1152/ajpcell.1985.248.3.C203. [DOI] [PubMed] [Google Scholar]
  18. Worley P. F., Baraban J. M., Colvin J. S., Snyder S. H. Inositol trisphosphate receptor localization in brain: variable stoichiometry with protein kinase C. Nature. 1987 Jan 8;325(7000):159–161. doi: 10.1038/325159a0. [DOI] [PubMed] [Google Scholar]
  19. Worley P. F., Baraban J. M., Supattapone S., Wilson V. S., Snyder S. H. Characterization of inositol trisphosphate receptor binding in brain. Regulation by pH and calcium. J Biol Chem. 1987 Sep 5;262(25):12132–12136. [PubMed] [Google Scholar]
  20. Wu W. C., Walaas S. I., Nairn A. C., Greengard P. Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes. Proc Natl Acad Sci U S A. 1982 Sep;79(17):5249–5253. doi: 10.1073/pnas.79.17.5249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yoshimasa T., Sibley D. R., Bouvier M., Lefkowitz R. J., Caron M. G. Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation. Nature. 1987 May 7;327(6117):67–70. doi: 10.1038/327067a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES