Protein Phosphorylation in the Nervous System

  • Manfred W. Kilimann
Conference paper
Part of the NATO ASI Series book series (volume 56)

Abstract

Protein phosphorylation is involved in many mechanisms that contribute to neuronal plasticity, i.e. in the modulation of the information processing and storage properties of nerve cells resulting, ultimately, in the ability of the nervous system to learn. At the molecular and cellular level, this means that a signal passing through a neuron leaves behind a trace that affects the future behaviour of the cell. The time scale of such an effect may be very different: it may last for only a few seconds, or it may be lifelong.

Keywords

Tyrosine Hydroxylase Protein Phosphorylation Inositol Trisphosphate Tyrosine Hydroxylase Gene Inositol Trisphosphate Receptor 
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. Bähler Mr Benfenati F, Valtorta F, Greengard P (1990) The synapsins and the regulation of synaptic function. BioEssays 12: 259–263PubMedCrossRefGoogle Scholar
  2. Black IB, Adler JE, Dreyfus CF, Friedman WF, LaGamma EF, Roach AH (1987) Biochemistry of information storage in the nervous system.Science 236: 1263–1268Google Scholar
  3. Campbell DG, Hardie DG, Vulliet PR (1986) Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase. J Biol Chem 261: 10489–10492PubMedGoogle Scholar
  4. Catterall WA (1988) Structure and function of voltage-sensitive ion channels. Science 242: 50–61PubMedCrossRefGoogle Scholar
  5. da Cunha A, Vitkovic L (1990) Regulation of immunoreactive GAP- 43 expression in rat cortical macroglia is cell type specific. J Cell Biol 111: 209–215PubMedCrossRefGoogle Scholar
  6. Dash KD, Hochner B, Kandel ER (1990) Injection of the cAMP- responsive element into the nucleus of Aplysia sensory neurons blocks long-term facilitation. Nature 345: 718–721PubMedCrossRefGoogle Scholar
  7. Hausdorff WP, Caron MG, Lefkowitz RJ (1990) Turning off the signal: desensitization of 6-adrenergic receptor function. FASEB J 4: 2881–2889PubMedGoogle Scholar
  8. Haycock JW (1990) Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. J Biol Chem 265: 11682–11691PubMedGoogle Scholar
  9. Hemmings HC, Nairn AC, McGuinnes T, Huganir RL, Greengard P (1989) Role of protein phosphorylation in neuronal signal transduction. FASEB J 3: 1583–1592PubMedGoogle Scholar
  10. Huganir RL, Greengard P (1990) Regulation of neurotransmitter receptor desensitization by protein phosphorylation. Neuron 5: 555–567PubMedCrossRefGoogle Scholar
  11. Nicoll RA (1988) The coupling of neurotransmitter receptors to ion channels in the brain. Science 241: 545–551PubMedCrossRefGoogle Scholar
  12. Sheng M, Greenberg ME (1990) The regulation and function of c- fos and other immediate early genes in the nervous system. Neuron 4: 477–485PubMedCrossRefGoogle Scholar
  13. Shuster MJ, Camardo JS, Siegelbaum SA, Kandel ER (1985) Cyclic AMP-dependent protein kinase closes the serotonin-sensitive K channels of Aplysia sensory neurones in cell-free membrane patches. Nature 313: 392–395PubMedCrossRefGoogle Scholar
  14. Supattapone S, Danoff SK, Theibert A, Joseph SK, Steiner J, Snyder SH (1988) Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium. Proc Natl Acad Sci USA 85:8747–8750PubMedCrossRefGoogle Scholar
  15. Wisden W, Errington ML, Williams S, Dunnett SB, Waters C, Hitchcock D, Evan G, Bliss TVP, Hunt SP (1990) Differential expression of immediate early genes in the hippocampus and spinal cord. Neuron 4: 603–614PubMedCrossRefGoogle Scholar
  16. Valiquette M, Bonin H, Hnatowich M, Caron MG, Lefkowitz RJ, Bouvier M (1990) Involvement of tyrosine residues located in the carboxyl tail of the human B-adrenergic receptor in agonist-induced down-regulation of the receptor. Proc Natl Acad Sci USA 87: 5089–5093PubMedCrossRefGoogle Scholar
  17. Zigmond RE (1985) Biochemical consequences of synaptic stimulation: The regulation of tyrosine hydroxylase activity by multiple transmitters. Trends in Neurosci 1985: 63–69CrossRefGoogle Scholar
  18. Zuber MX, Goodman DW, Karns LR, Fishman MC (1989) The neuronal growth-associated protein GAP-43 induces filopodia in non- neuronal cells. Science 244: 1193–1195PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Manfred W. Kilimann
    • 1
  1. 1.Institut für Physiologische Chemie (Abteilung für Biochemie Supramolekularer Systeme)Ruhr-Universität BochumBochum 1Germany

Personalised recommendations