2010年2月
Fbxo45, a Novel Ubiquitin Ligase, Regulates Synaptic Activity
JOURNAL OF BIOLOGICAL CHEMISTRY
- 巻
- 285
- 号
- 6
- 開始ページ
- 3840
- 終了ページ
- 3849
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M109.046284
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
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.
- リンク情報
- ID情報
-
- DOI : 10.1074/jbc.M109.046284
- ISSN : 0021-9258
- PubMed ID : 19996097
- Web of Science ID : WOS:000275254000037