Direct interaction of N-ethylmaleimide-sensitive factor with GABA A receptor β subunits

Hidefumi Goto, Miho Terunuma, Takashi Kanematsu, Yoshio Misumi, Stephen J. Moss, Masato Hirata

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)197-206
Number of pages10
JournalMolecular and Cellular Neuroscience
Issue number2
Publication statusPublished - Oct 2005

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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