TY - JOUR
T1 - Direct interaction of N-ethylmaleimide-sensitive factor with GABA A receptor β subunits
AU - Goto, Hidefumi
AU - Terunuma, Miho
AU - Kanematsu, Takashi
AU - Misumi, Yoshio
AU - Moss, Stephen J.
AU - Hirata, Masato
N1 - Funding Information:
We thank all the members in the laboratory for valuable discussions. This work was supported by the Japan–United Kingdom Research Co-operative Program of the Japan Society for the Promotion of Sciences (JSPS) and by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (MT, TK, and MH), the Japan Epilepsy Research Foundation (MH), the Novartis Foundation (Japan) for the Promotion of Science (MH), and the Kato Memorial Bioscience Foundation (TK).
PY - 2005/10
Y1 - 2005/10
N2 - GABAA receptors mediate most of the fast inhibitory neurotransmission in the brain, and are believed to be composed mainly of α, β, and γ subunits. It has been shown that GABAA receptors interact with a number of binding partners that act to regulate both receptor function and cell surface stability. Here, we reveal that GABA A receptors interact directly with N-ethylmaleimide-sensitive factor (NSF), a critical regulator of vesicular dependent protein trafficking, as measured by in vitro protein binding and co-immunoprecipitation assays. In addition, we established that NSF interacts with residues 395-415 of the receptor β subunits and co-localizes with GABAA receptors in hippocampal neurons. We also established that NSF can regulate GABAA receptor cell surface expression depending upon residues 395-415 in the β3 subunit. Together, our results suggest an important role for NSF activity in regulating the cell surface stability of GABAA receptors.
AB - GABAA receptors mediate most of the fast inhibitory neurotransmission in the brain, and are believed to be composed mainly of α, β, and γ subunits. It has been shown that GABAA receptors interact with a number of binding partners that act to regulate both receptor function and cell surface stability. Here, we reveal that GABA A receptors interact directly with N-ethylmaleimide-sensitive factor (NSF), a critical regulator of vesicular dependent protein trafficking, as measured by in vitro protein binding and co-immunoprecipitation assays. In addition, we established that NSF interacts with residues 395-415 of the receptor β subunits and co-localizes with GABAA receptors in hippocampal neurons. We also established that NSF can regulate GABAA receptor cell surface expression depending upon residues 395-415 in the β3 subunit. Together, our results suggest an important role for NSF activity in regulating the cell surface stability of GABAA receptors.
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U2 - 10.1016/j.mcn.2005.07.006
DO - 10.1016/j.mcn.2005.07.006
M3 - Article
C2 - 16095914
AN - SCOPUS:24944493275
SN - 1044-7431
VL - 30
SP - 197
EP - 206
JO - Molecular and Cellular Neurosciences
JF - Molecular and Cellular Neurosciences
IS - 2
ER -