β-Adrenergic regulation of synaptic NMDA receptors by cAMP-dependent protein kinase

Indira M. Raman, Gang Tong, Craig E. Jahr

Research output: Contribution to journalArticle

242 Scopus citations

Abstract

To identity the protein kinases regulating synaptic NMDA receptors, as well as the conditions favoring enhancement of NMDA receptor-mediated excitatory postsynaptic currents (EPSCs) by phosphorylation, we studied the effects of kinase activation and inhibition in hippocampal neurons. Inhibition of cAMP-dependent protein kinase (PKA) prevented recovery of NMDA receptors from calcineurin-mediated dephosphorylation induced by synaptic activity, suggesting that tonically active PKA phosphorylates receptors during quiescent periods. Conversely, elevation of PKA activity by forskolin, cAMP analogs, or the β-adrenergic receptor agonists norepinephrine and isoproterenol overcame the ability of calcineurin to depress the amplitude of NMDA EPSCs. Thus, stimulation of β-adrenergic receptors during excitatory synaptic transmission can increase charge transfer and Ca2+ influx through NMDA receptors.

Original languageEnglish (US)
Pages (from-to)415-421
Number of pages7
JournalNeuron
Volume16
Issue number2
DOIs
StatePublished - Feb 1996

ASJC Scopus subject areas

  • Neuroscience(all)

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