Neuronal protein phosphorylation: recent studies concerning protein I, a synapse-specific phosphoprotein

Pharmacol Biochem Behav. 1980:13 Suppl 1:169-74. doi: 10.1016/s0091-3057(80)80027-x.

Abstract

Recent studies are described concerning the physiological role and tissue distribution of Protein I, a synapse-specific phosphoprotein. This protein is present in both the central and the peripheral nervous system and appears to be enriched in synaptic vesicles. It is a major substrate for both Ca2(-)- and cyclic AMP-dependent phosphorylation in the brain. In slices of the facial motor nucleus from rat brainstem, serotonin (5-HT) added to the incubation medium stimulates the phosphorylation of Protein I. This effect is potentiated by low concentrations of isobutylmethylxanthine and is prevented by the serotonin antagonist mianserin.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Cyclic AMP / metabolism
  • Mianserin / pharmacology
  • Nerve Tissue Proteins / metabolism*
  • Nervous System / metabolism
  • Neurons / metabolism*
  • Neurotransmitter Agents / pharmacology
  • Phosphorylation
  • Serotonin / physiology
  • Synapses / physiology
  • Synapsins
  • Synaptic Membranes / metabolism

Substances

  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Synapsins
  • Mianserin
  • Serotonin
  • Cyclic AMP