Distinct γ2 Subunit Domains Mediate Clustering and Synaptic Function of Postsynaptic GABAAReceptors and Gephyrin
Gephyrin
Postsynaptic density
DOI:
10.1523/jneurosci.4011-04.2005
Publication Date:
2005-01-19T18:42:55Z
AUTHORS (5)
ABSTRACT
Modulation of the concentration postsynaptic GABA A receptors contributes to functional plasticity inhibitory synapses. The γ2 subunit receptor is specifically required for clustering these receptors, recruitment submembrane scaffold protein gephyrin sites, and function GABAergic To elucidate this mechanism, we here have mapped domains restoration in mutant neurons. Transfection -/- neurons with but not α2 rescues results restores amplitude frequency miniature currents wild-type levels. Analogous analyses chimeric γ2/α2 constructs indicate, unexpectedly, that fourth transmembrane domain sufficient whereas cytoplasmic are dispensable. In contrast, both major loop contribute efficient clusters essential IPSCs. Our study points a novel mechanism involved targeting
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