NSF Binding to GluR2 Regulates Synaptic Transmission
NSF Binding to GluR2 Regulates Synaptic Transmission
Here, we show that N-ethylmaleimide-sensitive fusion protein (NSF) interacts directly and selectively with the intracellular C-terminal domain of the GluR2 subunit of AMPA receptors. The interaction requires all three domains of NSF but occurs between residues Lys-844 and Gln-853 of rat GluR2, with Asn-851 playing a critical role. Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. This reduction in synaptic transmission was also observed when an anti-NSF monoclonal antibody (mAb) was loaded into CA1 neurons. These results demonstrate a previously unsuspected direct interaction in the postsynaptic neuron between two major proteins involved in synaptic transmission and suggest a rapid NSF-dependent modulation of AMPA receptor function.
- Kyoto University Japan
- University of Bristol United Kingdom
- Newcastle University United Kingdom
- University of Tokyo Japan
- Tokyo University of Pharmacy and Life Sciences Japan
Neurons, Neuroscience(all), Molecular Sequence Data, Vesicular Transport Proteins, Antibodies, Monoclonal, Excitatory Postsynaptic Potentials, Hippocampus, Synaptic Transmission, Rats, Receptors, Glutamate, Excitatory Amino Acid Agonists, Animals, Amino Acid Sequence, Receptors, AMPA, Rats, Wistar, Carrier Proteins, N-Ethylmaleimide-Sensitive Proteins, alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid, Cells, Cultured
Neurons, Neuroscience(all), Molecular Sequence Data, Vesicular Transport Proteins, Antibodies, Monoclonal, Excitatory Postsynaptic Potentials, Hippocampus, Synaptic Transmission, Rats, Receptors, Glutamate, Excitatory Amino Acid Agonists, Animals, Amino Acid Sequence, Receptors, AMPA, Rats, Wistar, Carrier Proteins, N-Ethylmaleimide-Sensitive Proteins, alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid, Cells, Cultured
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