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Proc Natl Acad Sci U S A. 2016 Aug 16;113(33):E4920-7. doi: 10.1073/pnas.1610631113. Epub 2016 Aug 1.

Extensive phosphorylation of AMPA receptors in neurons.

Author information

1
Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205;
2
Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205; Kavli Neuroscience Discovery Institute, Johns Hopkins University, Baltimore, MD 21205 rhuganir@jhmi.edu.

Abstract

Regulation of AMPA receptor (AMPAR) function is a fundamental mechanism controlling synaptic strength during long-term potentiation/depression and homeostatic scaling. AMPAR function and membrane trafficking is controlled by protein-protein interactions, as well as by posttranslational modifications. Phosphorylation of the GluA1 AMPAR subunit at S845 and S831 play especially important roles during synaptic plasticity. Recent controversy has emerged regarding the extent to which GluA1 phosphorylation may contribute to synaptic plasticity. Here we used a variety of methods to measure the population of phosphorylated GluA1-containing AMPARs in cultured primary neurons and mouse forebrain. Phosphorylated GluA1 represents large fractions from 12% to 50% of the total population under basal and stimulated conditions in vitro and in vivo. Furthermore, a large fraction of synapses are positive for phospho-GluA1-containing AMPARs. Our results support the large body of research indicating a prominent role of GluA1 phosphorylation in synaptic plasticity.

KEYWORDS:

AMPA receptor; excitatory synapse; protein kinase A; protein kinase C; synaptic plasticity

PMID:
27482106
PMCID:
PMC4995952
DOI:
10.1073/pnas.1610631113
[Indexed for MEDLINE]
Free PMC Article

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