Advertisement

Control of Translation by Regulation of Protein Phosphorylation and Dephosphorylation

  • Odd Nygård
  • Peter Westermann
Chapter
  • 62 Downloads

Abstract

The activity of a seemingly exponentially increasing number of well characterized, specific enzymes and enzyme systems has been shown to be regulated by phosphorylation and dephosphorylation of their constituent peptides. Depending on the specific enzyme system, increased phosphorylation may cause either a decrease or an increase in enzymatic activity. Cognately with this change in enzymatic activity, a large number of phosphorylated peptides can be detected in extract from intact cells or cell lysates. Subtle to dramatic changes in the phosphorylation state of a single given target protein may be brought about by a variety of components or conditions, such as hormones and growth factors, camp, temperature and nutrients or virus infection that affect the biochemistry and physiology of intact cells. These types of observations have led to the hypothesis that protein phosphorylation and dephosphorylation reactions constitute a primary regulatory mechanism in eukaryotic cells.

Keywords

Protein Phosphatase Cold Spring Harbor Antigen Peptide Limited Proteolysis High Performance Liquid Chromato 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Branton, D., Cohen, C.M., and Tyler, J. (1981) Cell 24, 24–32.PubMedCrossRefGoogle Scholar
  2. Brautigen, D.L., Ballou, L.M., and Fischer, F..H. (1982) Biochemistry 21, 1977–1982.CrossRefGoogle Scholar
  3. Clemens, M.J., Pain, V.M., Wong, S-T., and Henshaw, E.C. (1982) Nature 296, 93–95.PubMedCrossRefGoogle Scholar
  4. Farrell, P.J., Balkow, K., Hunt. T., Jackson, R., and Trachsel, H. (1977) Cell 11, 187–200.PubMedCrossRefGoogle Scholar
  5. Fullilove, S., Wollny, E., Stearns, G., Chen, S.-C., Kramer, G., and Hardesty, B. (1983) manuscript submitted.Google Scholar
  6. Grankowski, N., Lehmusvirta, D., Kramer, G., and Hardesty, B. (1980a) J. Biol. Chem.255, 310–316.PubMedGoogle Scholar
  7. Grankowski, N., Lehusvirta. D., Stearns, G., Kramer,C., and Hardesty,B. (1980b) J. Biol. Chem. 255, 5755–5762.PubMedGoogle Scholar
  8. Grosfeld, H., and 0choa, S. (1980) Proc. Natl. Acad. Sci.USA 77, 6526–6530.PubMedCrossRefGoogle Scholar
  9. Gross, M., and Mendelewski, J. (1978) Biochim. Biophys. Acta 520, 650–663.PubMedGoogle Scholar
  10. Hardesty, B., and Kramer, G. (1981) in Protein Phosphorylation: Cold Spring Harbor Conferences on Cell Proliferation Vol.8 ( Rosen,O.M., and Krebs,E.C., eds ). Cold Spring Harbor, pp. 959–977.Google Scholar
  11. Hemmings, E.A., Yellowlces, D., Kernohan, J.C., and Cohen, P. (1981) Eur. J. Biochem. 119, 443–451.PubMedCrossRefGoogle Scholar
  12. Hemmings, B. A., Resink, T.J., and Cohen, P. (1982) FEBS Lett. 150, 319–324.PubMedCrossRefGoogle Scholar
  13. Jackson, R.J., Herbert, P., Campbell, E.A., and Hunt, T. (1983) Eur. J. Bopchem. 131, 313–324.Google Scholar
  14. Jarett, L., Kiechle. F.L., and Parker, J.C.(1982) Fed. Proc. 41, 2736–2741.PubMedGoogle Scholar
  15. Krebs, E.G., and Beavo, J.A. (1979) Ann. Rev. Biochem. 48, 923–959.PubMedCrossRefGoogle Scholar
  16. Lee, E.Y.C., Silberman, S.R., Cranapathi, M.K., Petrovic, S., and Paris, H. (1980) in Advances in Cyclic Nucleotide Research Vol.13(Greengard,P., and Robison,G.A.,eds) Raven Press, New York, pp. 95–131.Google Scholar
  17. Levin, D.H., Petryshyn, R., and London, I.M. (1981) J. Biol. Chem. 256, 7638–7641.PubMedGoogle Scholar
  18. Litman,D.,Hsu,C.J., and Marchcsi,V.T. (1980) J. Cell. Sci. 42, 1–22.PubMedGoogle Scholar
  19. London, L.M., Ernst, V., Fagard, R., Lerourx, A., Levin, H. and Petryshyn, R.(1981) in Protein Phosphorylation: Cold Spring Harbor Conferences on Cell Proliferation, Vol.8 (Rosen,0.M., and Krebs,E.G., eds.) Cold Spring Harbor, pp.941–958.Google Scholar
  20. Mitsui, K.-I., Datta. A., and Ochoa, S. (1981) Proc. Natl. Acad. Sci. USA 78, 4128–4132.PubMedCrossRefGoogle Scholar
  21. Ochoa. S., Siekierka, J., Mitsui, K., deHaro, C., and Grosfeld, H (1981) in Protein Phosphorylation: Cold Spring Harbor Conferences on Cell Proliferation, Vol.8 (Rosen,O.M., and Krebs,E.G., eds.) Cold Spring Harbor, pp. 931–940.Google Scholar
  22. Ranu, R.S., and London, I.M. (1976) Proc. Natl. Acad. Sci. USA 73, 4349–4353.PubMedCrossRefGoogle Scholar
  23. Samuel, C.E. (1979) Proc. Natl. Acad. Sci. USA 76, 600–604.PubMedCrossRefGoogle Scholar
  24. Seals, J.R., and Czech, M.P. (1982) Fed. Proc. 41, 2730–2735.PubMedGoogle Scholar
  25. Shotton. D.M., Burke, B.E., and Branton, D. (1979) J. Mol. Biol. 131, 303–329.PubMedCrossRefGoogle Scholar
  26. Sierkierka, J., Mause, L., and Ochoa,S. (1982) Proc. Natl. Acad. Sci. USA 79, 2537–2540.CrossRefGoogle Scholar
  27. Towbin, H., Staehelin, T., and Gordon, J. (1979) Proc. Natl. Acad. Sci. USA 76, 4350–4354.CrossRefGoogle Scholar
  28. Trachel, H., Ranu, R.S., and London, I.M. (1978) Proc. Natl. Acad. Sci. USA 74, 3654–3658.CrossRefGoogle Scholar
  29. Traugh, J.A. (1981) in Biochemical Actions of Hormones, Vol. VIII (Litwack, G. ed.) Academic Press, New York, pp. 167–208.Google Scholar
  30. Vandenheede, J.R., Yang, S.-D., Goris, J., and Merlevede, W. (1980) J. Biol. Chem. 255, 11768–11774.PubMedGoogle Scholar
  31. Wallis, M.H., Kramer, G., and Hardesty, B. (1980) Biochemistry 12, 798–804.CrossRefGoogle Scholar
  32. Wo11ny, E., Watkins, K., Kramer, G., and Hardesty, B. (1983) Manuscript submitted.Google Scholar
  33. Yang, S.-D., Vandenhcede, J.R., Goris, J., and Merlevede, W. (1980) J. Biol. Chem. 255, 11759–11767.PubMedGoogle Scholar
  34. Yang, S.-D., Vandenheede, J.R., and Merlevede, W. (1981) J. Biol. Chem. 256, 10231–10234.PubMedGoogle Scholar
  35. Zardeneta, G., Kramer, G., and Hardesty, B. (1982) Proc. Natl. Acad. Sci. USA 79, 3158–3161.PubMedCrossRefGoogle Scholar

Copyright information

© The Human Press Inc. 1983

Authors and Affiliations

  • Odd Nygård
    • 1
  • Peter Westermann
    • 2
  1. 1.The Wenner-Gren InstituteUniversity of StockholmStockholmSweden
  2. 2.Central Institute of Molecular BiologyAcademy of Sciences of GDRBerlin-BuchGermany

Personalised recommendations