s-nitro-n-acetylpenicillamine and glycinaldehyde

Postsynaptic AMPA receptor (AMPAR) trafficking mediates some forms of synaptic plasticity that are modulated by NMDA receptor (NMDAR) activation and N-ethylmaleimide sensitive factor (NSF). We report that NSF is physiologically S-nitrosylated by endogenous, neuronally derived nitric oxide (NO). S-nitrosylation of NSF augments its binding to the AMPAR GluR2 subunit. Surface insertion of GluR2 in response to activation of synaptic NMDARs requires endogenous NO, acting selectively upon the binding of NSF to GluR2. Thus, AMPAR recycling elicited by NMDA neurotransmission is mediated by a cascade involving NMDA activation of neuronal NO synthase to form NO, leading to S-nitrosylation of NSF which is thereby activated, enabling it to bind to GluR2 and promote the receptor's surface expression.

Topics: Adenylyl Imidodiphosphate; Aldehydes; Animals; Blotting, Western; Cells, Cultured; Cerebellum; Cysteine; Diagnostic Imaging; Dizocilpine Maleate; Drug Interactions; Embryo, Mammalian; Enzyme Activation; Enzyme Inhibitors; Epoxy Compounds; Ethylmaleimide; Excitatory Amino Acid Antagonists; Gene Expression Regulation; Hippocampus; Immunoprecipitation; Mice; Mice, Knockout; Mutagenesis; N-Ethylmaleimide-Sensitive Proteins; Nerve Tissue Proteins; Neurons; NG-Nitroarginine Methyl Ester; Nitric Oxide; Nitric Oxide Donors; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Penicillamine; Protein Binding; Rats; Receptors, AMPA; Recombinant Fusion Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Reagents; Time Factors; Transfection; Vesicular Transport Proteins