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Cornichon proteins determine the subunit composition of synaptic AMPA receptors.

Authors
Herring, BE; Shi, Y; Suh, YH; Zheng, CY; Blankenship, SM; Roche, KW; Nicoll, RA
Citation
Neuron, 77(6):1083-1096, 2013
Journal Title
Neuron
ISSN
0896-62731097-4199
Abstract
Cornichon-2 and cornichon-3 (CNIH-2/-3) are AMPA receptor (AMPAR) binding proteins that promote receptor trafficking and markedly slow AMPAR deactivation in heterologous cells, but their role in neurons is unclear. Using CNIH-2 and CNIH-3 conditional knockout mice, we find a profound reduction of AMPAR synaptic transmission in the hippocampus. This deficit is due to the selective loss of surface GluA1-containing AMPARs (GluA1A2 heteromers), leaving a small residual pool of synaptic GluA2A3 heteromers. The kinetics of AMPARs in neurons lacking CNIH-2/-3 are faster than those in WT neurons due to the fast kinetics of GluA2A3 heteromers. The remarkably selective effect of CNIHs on the GluA1 subunit is probably mediated by TARP γ-8, which prevents a functional association of CNIHs with non-GluA1 subunits. These results point to a sophisticated interplay between CNIHs and γ-8 that dictates subunit-specific AMPAR trafficking and the strength and kinetics of synaptic AMPAR-mediated transmission.
MeSH terms
AnimalsAnimals, NewbornCells, CulturedExcitatory Postsynaptic Potentials/*physiologyHippocampus/physiologyMiceMice, KnockoutOrgan Culture TechniquesProtein Subunits/chemistry/physiologyReceptors, AMPA/*chemistry/*physiologySynapses/chemistry/physiologySynaptic Transmission/*physiology
DOI
10.1016/j.neuron.2013.01.017
PMID
23522044
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pharmacology
AJOU Authors
서, 영호
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