Journal of Neuroscience 2013-05-15

Dendritic GluN2A synthesis mediates activity-induced NMDA receptor insertion.

Sharon A Swanger, Yuncen A He, Joel D Richter, Gary J Bassell

Index: J. Neurosci. 33(20) , 8898-908, (2013)

Full Text: HTML

Abstract

Long-term synaptic plasticity involves changes in the expression and membrane insertion of cell-surface proteins. Interestingly, the mRNAs encoding many cell-surface proteins are localized to dendrites, but whether dendritic protein synthesis is required for activity-induced surface expression of specific proteins is unknown. Herein, we used microfluidic devices to demonstrate that dendritic protein synthesis is necessary for activity-induced insertion of GluN2A-containing NMDA receptors in rat hippocampal neurons. Furthermore, visualization of activity-induced local translation of GluN2A mRNA and membrane insertion of GluN2A protein in dendrites was directly observed and shown to depend on a 3' untranslated region cytoplasmic polyadenylation element and its associated translation complex. These findings uncover a novel mechanism for cytoplasmic polyadenylation element-mediated posttranscriptional regulation of GluN2A mRNA to control NMDA receptor surface expression during synaptic plasticity.

Related Compounds

Structure Name/CAS No. Articles
Glycine Structure Glycine
CAS:56-40-6
Glycine HCl Structure Glycine HCl
CAS:6000-43-7
Anisomycin Structure Anisomycin
CAS:22862-76-6