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演題詳細

Symposium

快・不快情動を生成し記憶する脳内メカニズム
Mechanisms controlling expression and memory of emotions

開催日 2014/9/11
時間 14:00 - 16:00
会場 Room D(503)
Chairperson(s) 貝淵 弘三 / Kozo Kaibuchi (名古屋大学大学院医学系研究科 / Nagoya University Graduate School of Medicine, Japan)
南 雅文 / Masabumi Minami (北海道大学大学院薬学研究院薬理学研究室 / Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Japan)

リン酸化プロテオミクスによるモノアミンシグナルの解析
Phosphoproteomic analysis of monoamine signals to understand the monoamine actions

  • S1-D-1-5
  • 貝淵 弘三 / Kozo Kaibuchi:1 
  • 1:名古屋大学 / Nagoya University, Japan 

Emotions such as pleasure, displeasure and fear are controlled by monoaminergic neurons. The mono-amine-mediated reward process is broadly conserved from nematodes to humans. Although the roles of some intracellular signals of monoamines are becoming clear, many questions about the intracellular signals that are relevant to emotions remain largely unknown. We aim to uncover information that will allow us to understand the mechanisms that control emotions, thereby clarifying the machineries that regulate the operating principles of neural circuits and their re-structuring. We are currently comprehensively analyzing phosphorylation reactions in specific brain regions, such as the nucleus accumbens, upon pleasant sensations and specifying the signaling pathways involved in emotion control. We have found that more than a hundred proteins are specifically phosphorylated upon stimulation by D1 receptor agonists through the action of protein kinase A or MAP kinase. We discuss the recent progress of phosphoproteomic analysis of monoamine signals in this symposium.

A part of this study is the result of " Bioinformatics for brain sciences" carried out under the Strategic Research Program for Brain Sciences by the Ministry of Education, Culture, Sports, Science and Technology of Japan.

Ref.

Amano M., Tsumura Y., Taki K., Harada H., Mori K., Nishioka T., Kato K., Suzuki T., Nishioka Y., Iwamatsu A. & Kaibuchi K., A proteomic approach for comprehensively screening substrates of protein kinases such as Rho-kinase. PLoS One 5, 2010, e8704

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