Fbxo45, a novel ubiquitin ligase, regulates synaptic activity

Hirobumi Tada, Hirotaka James Okano, Hiroshi Takagi, Shinsuke Shibata, Ikuko Yao, Masaki Matsumoto, Toru Saiga, Keiichi I. Nakayama, Haruo Kashima, Takuya Takahashi, Mitsutoshi Setou, Hideyuki Okano

Research output: Contribution to journalArticlepeer-review

67 Citations (Scopus)


Neurons communicate with each other through synapses. To establish the precise yet flexible connections that make up neural networks in the brain, continuous synaptic modulation is required. The ubiquitin-proteasome system of protein degradation is one of the critical mechanisms that underlie this process, playing crucial roles in the regulation of synaptic structure and function. We identified a novel ubiquitin ligase, Fbxo45, that functions at synapses. Fbxo45 is evolutionarily conserved and selectively expressed in the nervous system. We demonstrated that the knockdown of Fbxo45 in primary cultured hippocampal neurons resulted in a greater frequency of miniature excitatory postsynaptic currents. We also found that Fbxo45 induces the degradation of a synaptic vesicle-priming factor, Munc13-1.We propose that Fbxo45 plays an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse.

Original languageEnglish
Pages (from-to)3840-3849
Number of pages10
JournalJournal of Biological Chemistry
Issue number6
Publication statusPublished - 2010 Feb 5

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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