Dynamic Regulation of N-Methyl-d-aspartate (NMDA) and α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by Posttranslational Modifications

J Biol Chem. 2015 Nov 27;290(48):28596-603. doi: 10.1074/jbc.R115.652750. Epub 2015 Oct 9.

Abstract

Many molecular mechanisms underlie the changes in synaptic glutamate receptor content that are required by neuronal networks to generate cellular correlates of learning and memory. During the last decade, posttranslational modifications have emerged as critical regulators of synaptic transmission and plasticity. Notably, phosphorylation, ubiquitination, and palmitoylation control the stability, trafficking, and synaptic expression of glutamate receptors in the central nervous system. In the current review, we will summarize some of the progress made by the neuroscience community regarding our understanding of phosphorylation, ubiquitination, and palmitoylation of the NMDA and AMPA subtypes of glutamate receptors.

Keywords: N-methyl-D-aspartate receptor (NMDA receptor, NMDAR); alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPA receptor, AMPAR); glutamate receptor; post-translational modification (PTM); protein palmitoylation; ubiquitin.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Lipoylation / physiology*
  • Phosphorylation / physiology
  • Protein Transport / physiology
  • Receptors, AMPA / metabolism*
  • Receptors, N-Methyl-D-Aspartate / metabolism*
  • Ubiquitination / physiology*

Substances

  • Receptors, AMPA
  • Receptors, N-Methyl-D-Aspartate