Ontology highlight
ABSTRACT:
SUBMITTER: Kneussel M
PROVIDER: S-EPMC26993 | biostudies-literature | 2000 Jul
REPOSITORIES: biostudies-literature
Kneussel M M Haverkamp S S Fuhrmann J C JC Wang H H Wässle H H Olsen R W RW Betz H H
Proceedings of the National Academy of Sciences of the United States of America 20000701 15
gamma-Aminobutyric acid type A receptors (GABA(A)Rs) are ligand-gated chloride channels that exist in numerous distinct subunit combinations. At postsynaptic membrane specializations, different GABA(A)R isoforms colocalize with the tubulin-binding protein gephyrin. However, direct interactions of GABA(A)R subunits with gephyrin have not been reported. Recently, the GABA(A)R-associated protein GABARAP was found to bind to the gamma2 subunit of GABA(A)Rs. Here we show that GABARAP interacts with g ...[more]