Translation of striatal-enriched protein tyrosine phosphatase (STEP) after beta1-adrenergic receptor stimulation

J Neurochem. 2007 Oct;103(2):531-41. doi: 10.1111/j.1471-4159.2007.04749.x. Epub 2007 Jul 10.

Abstract

The beta-adrenergic system is implicated in long-term synaptic plasticity in the CNS, a process that requires protein synthesis. To identify proteins that are translated in response to beta-adrenergic receptor stimulation and the pathways that regulate this process, we investigated the effects of isoproterenol on the translation of striatal-enriched protein tyrosine phosphatase (STEP) in both cortico-striatal slices and primary neuronal cultures. Isoproterenol stimulation induced a rapid dose-dependent increase in STEP expression. Anisomycin blocked the increase in STEP expression while actinomycin D had no effect, suggesting a translation-dependent mechanism. Isoproterenol-induced STEP translation required activation of beta1-receptors. Application of the MAPK/ERK kinase (MEK) inhibitor SL327 blocked both isoproterenol-induced activation of pERK and subsequent STEP translation. Inhibitors of PI3K (LY294002) or mTOR (rapamycin) also completely blocked STEP translation. These results suggest that co-activation of both the ERK and PI3K-Akt-mTOR pathways are required for STEP translation. As one of the substrates of STEP includes ERK itself, these results suggest that STEP is translated upon beta-adrenergic activation as part of a negative feedback mechanism.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenergic alpha-1 Receptor Agonists*
  • Adrenergic beta-Agonists / pharmacology*
  • Animals
  • Blotting, Western
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Fluorescent Antibody Technique
  • Immunohistochemistry
  • Isoproterenol / pharmacology
  • Male
  • Mitogen-Activated Protein Kinase 1 / biosynthesis
  • Mitogen-Activated Protein Kinase 3 / biosynthesis
  • Neuronal Plasticity / drug effects
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein Biosynthesis / drug effects
  • Protein Kinases / biosynthesis
  • Protein Kinases / genetics
  • Protein Tyrosine Phosphatases, Non-Receptor / biosynthesis*
  • Protein Tyrosine Phosphatases, Non-Receptor / genetics
  • Proto-Oncogene Proteins c-akt / biosynthesis
  • Proto-Oncogene Proteins c-akt / genetics
  • Rats
  • Rats, Sprague-Dawley
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Subcellular Fractions / drug effects
  • Subcellular Fractions / metabolism
  • TOR Serine-Threonine Kinases
  • Transcription, Genetic / drug effects

Substances

  • Adrenergic alpha-1 Receptor Agonists
  • Adrenergic beta-Agonists
  • Protein Kinases
  • mTOR protein, rat
  • Proto-Oncogene Proteins c-akt
  • TOR Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Protein Tyrosine Phosphatases, Non-Receptor
  • Ptpn5 protein, rat
  • Isoproterenol