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
. 1978 Dec;75(12):5926–5930. doi: 10.1073/pnas.75.12.5926

Compartmentalization of cyclic AMP-dependent protein kinases in human erythrocytes.

G Dreyfuss, K J Schwartz, E R Blout
PMCID: PMC393089  PMID: 216002

Abstract

The human erythrocyte contains two types of cyclic AMP-dependent protein kinase. The membrane-associated protein kinase holoenzyme can be released intact by hypotonic treatment at alkaline pH. Chromatography on DEAE-cellulose and molecular weight determinations demonstrate that this enzyme is a type I cyclic AMP-dependent protein kinase, while the predominant cyclic AMP-dependent protein kinase found in the cytoplasm is type II. The catalytic subunits of the two types of kinase found in the erythrocyte are identical, but the regulatory subunits, which distinguish the two types of kinase, determine their localization within the cell. It is proposed that the regulatory subunit of the type I enzyme, in addition to binding the catalytic subunit, interacts specifically with one or more membrane proteins and that this interaction may serve to position the kinase in preferential proximity to protein substrates.

Full text

PDF
5926

Selected References

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

  1. Bechtel P. J., Beavo J. A., Krebs E. G. Purification and characterization of catalytic subunit of skeletal muscle adenosine 3':5'-monophosphate-dependent protein kinase. J Biol Chem. 1977 Apr 25;252(8):2691–2697. [PubMed] [Google Scholar]
  2. Boivin P., Galand C. Purification and characterization of an adenosine cyclic 3':5' monophosphate-dependent protein kinase from human erythrocyte membrane. Biochem Biophys Res Commun. 1978 Mar 30;81(2):473–480. doi: 10.1016/0006-291x(78)91558-9. [DOI] [PubMed] [Google Scholar]
  3. Corbin J. D., Keely S. L. Characterization and regulation of heart adenosine 3':5'-monophosphate-dependent protein kinase isozymes. J Biol Chem. 1977 Feb 10;252(3):910–918. [PubMed] [Google Scholar]
  4. Corbin J. D., Keely S. L., Park C. R. The distribution and dissociation of cyclic adenosine 3':5'-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues. J Biol Chem. 1975 Jan 10;250(1):218–225. [PubMed] [Google Scholar]
  5. Corbin J. D., Sugden P. H., Lincoln T. M., Keely S. L. Compartmentalization of adenosine 3':5'-monophosphate and adenosine 3':5'-monophosphate-dependent protein kinase in heart tissue. J Biol Chem. 1977 Jun 10;252(11):3854–3861. [PubMed] [Google Scholar]
  6. Costa M., Gerner E. W., Russell D. H. Cell cycle-specific activity of type I and type II cyclic adenosine 3':5'-monophosphate-dependent protein kinases in Chinese hamster ovary cells. J Biol Chem. 1976 Jun 10;251(11):3313–3319. [PubMed] [Google Scholar]
  7. Fairbanks G., Avruch J. Phosphorylation of endogenous substrates by erythrocyte membrane protein kinases. II. Cyclic adenosine monophosphate-stimulated reactions. Biochemistry. 1974 Dec 31;13(27):5514–5521. doi: 10.1021/bi00724a010. [DOI] [PubMed] [Google Scholar]
  8. Fuller D. J., Byus C. V., Russell D. H. Specific regulation by steroid hormones of the amount of type I cyclic AMP-dependent protein kinase holoenzyme. Proc Natl Acad Sci U S A. 1978 Jan;75(1):223–227. doi: 10.1073/pnas.75.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gharrett A. J., Malkinson A. M., Sheppard J. R. Cyclic AMP-dependent protein kinases from normal and SV40-transformed 3T3 cells. Nature. 1976 Dec 16;264(5587):673–675. doi: 10.1038/264673a0. [DOI] [PubMed] [Google Scholar]
  10. Gilman A. G. A protein binding assay for adenosine 3':5'-cyclic monophosphate. Proc Natl Acad Sci U S A. 1970 Sep;67(1):305–312. doi: 10.1073/pnas.67.1.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Guthrow C. E., Jr, Allen J. E., Rasmussen H. Phosphorylation of an endogenous membrane protein by an endogenous, membrane-associated cyclic adenosine 3',5'-monophosphate-dependent protein kinase in human erythrocyte ghosts. J Biol Chem. 1972 Dec 25;247(24):8145–8153. [PubMed] [Google Scholar]
  12. Haley B. E. Photoaffinity labeling of adenosine 3',5'-cyclic monophosphate binding sites of human red cell membranes. Biochemistry. 1975 Aug 26;14(17):3852–3857. doi: 10.1021/bi00688a018. [DOI] [PubMed] [Google Scholar]
  13. Hofmann F., Beavo J. A., Bechtel P. J., Krebs E. G. Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle. J Biol Chem. 1975 Oct 10;250(19):7795–7801. [PubMed] [Google Scholar]
  14. Hosey M. M., Tao M. An analysis of the autophosphorylation of rabbit and human erythrocyte membranes. Biochemistry. 1976 Apr 6;15(7):1561–1568. doi: 10.1021/bi00652a029. [DOI] [PubMed] [Google Scholar]
  15. Krebs E. G. Protein kinases. Curr Top Cell Regul. 1972;5:99–133. [PubMed] [Google Scholar]
  16. 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]
  17. Lee P. C., Radloff D., Schweppe J. S., Jungmann R. A. Testicular protein kinases. Characterization of multiple forms and ontogeny. J Biol Chem. 1976 Feb 25;251(4):914–921. [PubMed] [Google Scholar]
  18. Pomerantz A. H., Rudolph S. A., Haley B. E., Greengard P. Photoaffinity labeling of a protein kinase from bovine brain with 8-azidoadenosine 3',5'-monophosphate. Biochemistry. 1975 Aug 26;14(17):3858–3862. doi: 10.1021/bi00688a019. [DOI] [PubMed] [Google Scholar]
  19. Roses A. D., Appel S. H. Erythrocyte protein phosphorylation. J Biol Chem. 1973 Feb 25;248(4):1408–1411. [PubMed] [Google Scholar]
  20. Rubin C. S. Adenosine 3':5'-monophosphate-regulated phosphorylation of erythrocyte membrane proteins. Separation of membrane-associated cyclic adenosine 3':5'-monophosphate-dependent protein kinase from its endogenous substrates. J Biol Chem. 1975 Dec 10;250(23):9044–9052. [PubMed] [Google Scholar]
  21. Rubin C. S., Erlichman J., Rosen O. M. Cyclic adenosine 3',5'-monophosphate-dependent protein kinase of human erythrocyte membranes. J Biol Chem. 1972 Oct 10;247(19):6135–6139. [PubMed] [Google Scholar]
  22. Rubin C. S., Rosen O. M. Protein phosphorylation. Annu Rev Biochem. 1975;44:831–887. doi: 10.1146/annurev.bi.44.070175.004151. [DOI] [PubMed] [Google Scholar]
  23. Rubin C. S., Rosen O. M. The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes. Biochem Biophys Res Commun. 1973 Jan 23;50(2):421–429. doi: 10.1016/0006-291x(73)90857-7. [DOI] [PubMed] [Google Scholar]
  24. Singer S. J. Molecular biology of cellular membranes with applications to immunology. Adv Immunol. 1974;19(0):1–66. doi: 10.1016/s0065-2776(08)60251-5. [DOI] [PubMed] [Google Scholar]
  25. Srivastava A. K., Stellwagen R. H. Presence of the sites for interacting with cyclic AMP and with catalytic subunit on small fragments of protein kinase regulatory subunit. J Biol Chem. 1978 Mar 25;253(6):1752–1755. [PubMed] [Google Scholar]
  26. Steck T. L., Kant J. A. Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes. Methods Enzymol. 1974;31:172–180. doi: 10.1016/0076-6879(74)31019-1. [DOI] [PubMed] [Google Scholar]
  27. Sugden P. H., Holladay L. A., Reimann E. M., Corbin J. D. Purification and characterization of the catalytic subunit of adenosine 3':5'-cyclic monophosphate-dependent protein kinase from bovine liver. Biochem J. 1976 Nov;159(2):409–422. doi: 10.1042/bj1590409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Walter U., Uno I., Liu A. Y., Greengard P. Identification, characterization, and quantitative measurement of cyclic AMP receptor proteins in cytosol of various tissues using a photoaffinity ligand. J Biol Chem. 1977 Sep 25;252(18):6494–6500. [PubMed] [Google Scholar]
  29. Witt J. J., Roskoski R., Jr Rapid protein kinase assay using phosphocellulose-paper absorption. Anal Biochem. 1975 May 26;66(1):253–258. doi: 10.1016/0003-2697(75)90743-5. [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