Regulation of Cellular Functions by Phosphorylation and Dephosphorylation of Proteins: An Introduction

  • F. Hofmann
Part of the NATO Advanced Study Institutes Series book series (NSSA, volume 44)


During the last decade it has become apparent that activation of specific protein kinases by intracellular generated signals — such as calcium, cAMP, cGMP and other less well defined small molecules — and;concomitant phosphorylation of key regulatory proteins or enzymes is one important mechanism by which many hormones, neurotransmitters and autacoids (locally generated and acting hormones) regulate cellular functions. From the results obtained so far it is quite clear that protein phosphorylation is not the only regulatory mechanism triggered by the binding of hormones to plasma membrane receptors. This mechanism is only operative in such situations in which the cellular response follows hormone binding within seconds to minutes. This mechanism phosphorylation/dephosphorylation has not been observed in very fast responses (milliseconds) — presumably since the protein kinase catalyzed phophotransfer is too slow to modify a significant number of protein molecules before the onset of such fast cellular responses. In addition protein phosphorylation is not primarily involved in slow cellular responses occurring within hours — presumably since the covalent modification carried out by the protein kinase is not stable for hours but easily reversed by the action of one or several protein phosphatases. However, although the very fast and very slow cellular responses are not mediated by phosphorylation of some regulatory proteins, these responses may be modulated by the phosphorylation or dephosphorylation of some proteins involved in these responses.


Myosin Light Chain Kinase Phosphorylase Kinase Regulate Protein Kinase Actomyosin ATPase Specific Protein Kinase 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    P. B. Chock, S. G. Rhee and E. R. Stadtman, (1980) “Interconvertible enzyme cascades in cellular regulation” Ann. Rev. Biochem 49: 813–843.PubMedCrossRefGoogle Scholar
  2. 2.
    J. R. Knowles (1980) “Enzyme-catalyzed phosphoryltransfer reactions” Ann. Rev. Biochem 49: 877–919.PubMedCrossRefGoogle Scholar
  3. 3.
    E. G. Krebs and J. A. Beavo (1979) “Phosphorylation-dephosphorylation of enzymes” Ann. Rev. Biochem 48: 923–959.PubMedCrossRefGoogle Scholar
  4. 4.
    D. A. Walsh and R. H. Cooper (1979) “The physiological regulation and function of cAMP-dependent protein kinases” Biochem. Action of Hormones Vol. VI: 1–75.CrossRefGoogle Scholar
  5. 5.
    D. B. Glass and E. G. Krebs (1980) “Protein phosphorylation catalyzed by cyclic AMP-dependent and cyclic GMP-dependent protein kinases” Ann. Rev. Pharmacol. Toxicol 20: 363–388.CrossRefGoogle Scholar
  6. 6.
    G. N. Gill and R. W. McCaine (1979) “Guanosine-3’,5’-monophosphate-dependent protein kinase” Curr. Topic. Cell Reg 15: 1–45.Google Scholar
  7. 7.
    Th. R. Soderling (1979) “Regulatory functions of protein multi-site phosphorylation” Mol. Cell. Endocrinol 16: 157–180.PubMedCrossRefGoogle Scholar
  8. 8.
    C. Baglioni (1979) “Interferon-induced enzymatic activities and their role in the antiviral state” Cell 17: 255–264.PubMedCrossRefGoogle Scholar
  9. 9.
    B. R. G. Williams and J. M. Kerr (1980) “The 2–5 A (pppA2’p5’Rp) system in interferon-treated and control cells” TIBS p. 138–140.Google Scholar
  10. 10.
    R. H. Kretsinger (1980) “Structure and evolution of calcium-modulated proteins” CRC Crit. Rev. Biochem 8: 119–174.PubMedCrossRefGoogle Scholar
  11. 11.
    R. H. Kretsinger (1979) “The informational role of calcium in the cytosol” Advances Cyclic Nucleot. Res 11: 1–26.Google Scholar
  12. 12.
    D. J. Wolff and C. O. Brostrom (1979) “Properties and functions of the calcium-dependent regulator protein” Advances in Cyclic Nucleot. Res 11: 27–88.Google Scholar
  13. 13.
    A. R. Means and J. R. Dedman (1980) “Calmodulin–an intracellular calcium receptor” Nature 285: 73–76.PubMedCrossRefGoogle Scholar
  14. 14.
    J. H. Wang and D. M. Waisman (1979) “Calmodulin and its role in the second-messenger system” Curr. Topic. Cell. Regul 15: 47–107.Google Scholar
  15. 15.
    C. B. Klee, T. H. Crouch and P. G. Richman (1980) “Calmodulin” Ann. Rev. Biochem 49: 489–515.PubMedCrossRefGoogle Scholar
  16. 16.
    J. T. Stull (1980) “Phosphorylation of contractile proteins in relation to muscle function” Advances in Cyclic Nucleot. Res 13: 39–93.Google Scholar
  17. 17.
    R. S. Adelstein and E. Eisenberg (1980) “Regulation and kinetics of actin-myosin-ATP interaction” Ann. Rev. Biochem 49: 921–956.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1982

Authors and Affiliations

  • F. Hofmann
    • 1
  1. 1.Pharmakologisches Institut universität HeidelbergHeidelbergGermany

Personalised recommendations