Elucidation of the mechanism of the specific interaction of a mouse peptide pheromone ESP1 and the class-C GPCR receptor

• Project/Area Number: 24780104
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Applied biochemistry
• Research Institution: Kumamoto University
• Principal Investigator: YOSHINAGA Sosuke 熊本大学, 生命科学研究部, 助教 (00448515)
• Research Collaborator: TOUHARA Kazushige 東京大学, 大学院農学生命科学研究科, 教授 (00280925)
• Project Period (FY): 2012-04-01 – 2014-03-31
• Project Status: Completed (Fiscal Year 2013)
• Budget Amount: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000); Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000); Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
• Keywords: 情報伝達 / フェロモン / ＮＭＲ / 立体構造 / 相互作用 / マウス / ＧＰＣＲ / ぺプチド / 構造生物学 / タンパク質 / NMR / GPCR / 分子認識

Research Abstract

Animals communicate using "pheromones", which are tools for accurate recognition of the opposite sex, to preserve the species. Our collaborators, the Touhara group at the University of Tokyo, identified ESP1, which is a peptidic sex pheromone that is released in male mouse tear fluids and enhances female sexual receptive behavior (Nature, 2005). They also elucidated that ESP1 is selectively recognized by a specific class-C G-protein-coupled receptor (GPCR), V2Rp5, which is expressed in the vomeronasal organ that is located beneath the nasal septum (Nature, 2010).
We determined the three dimensional structure of ESP1, and revealed the binding mode between ESP1 and the receptor V2Rp5, based on these structures (JBC, 2013). To our knowledge, this is the first report of the structural information about the interaction between a mammalian peptide pheromone and its receptor.

Research Products

• [Journal Article] Expression and purification of mouse peptide ESP4 in Escherichia coil (2014)
  • Author(s): Hirakane M, Taniguchi M, Yoshinaga S, Misumi S, Terasawa H
  • Journal Title: Protein Expression and Purification Volume: 96 Pages: 20-25
  • DOI: 10.1016/j.pep.2014.01.010
  • Peer Reviewed
• [Journal Article] Backbone and side-chain ^1 H, ^<15> N and ^<13>C assignments of mouse peptide ESP4 (2014)
  • Author(s): Taniguchi, M., Yoshinaga, S., Haga-Yamanaka, H., Touhara, K., and Terasawa, H.
  • Journal Title: Biomolecular NMR Assignments Volume: 8 Issue: 1 Pages: 7-9
  • DOI: 10.1007/s12104-012-9441-7
  • Peer Reviewed
• [Journal Article] マウスの性行動を制御するペプチド性フェロモンESP1の立体構造決定―クラスCタイプGPCRによるリガンド認識機構の解析― (2014)
  • Author(s): 谷口雅浩,吉永壮佐,佐藤徹,はが紗智子,東原和成,寺沢宏明
  • Journal Title: 化学と生物 Volume: 52
  • NAID: 130004808939
  • Peer Reviewed
• [Journal Article] マウスの性行動を制御するペプチド性フェロモンESP1の立体構造決定―クラスＣタイプＧＰＣＲによるリガンド認識機構の解析― (2014)
  • Author(s): 谷口雅浩，吉永壮佐，佐藤徹，はが紗智子，東原和成，寺沢宏明
  • Journal Title: 化学と生物 Volume: 52 Pages: 67-69
  • NAID: 130004808939
  • Peer Reviewed
• [Journal Article] Structure of the Mouse Sex Peptide Pheromone ESP1 Reveals a Molecular Basis for Specific Binding to the Class C G-protein-coupled Vomeronasal Receptor (2013)
  • Author(s): Yoshinaga S, Sato T, Hirakane M, Esaki K, Hamaguchi T, Haga-Yamanaka S, Tsunoda M, Kimoto H, Shimada I, Touhara K, Terasawa H
  • Journal Title: The Journal of Biological Chemistry Volume: 288 Issue: 22 Pages: 16064-72
  • DOI: 10.1074/jbc.m112.436782
  • Peer Reviewed
• [Journal Article] Backbone and side-chain 1H, 15N and 13C assignments of mouse peptide ESP4. (2013)
  • Author(s): Taniguchi, M., Yoshinaga, S., Haga-Yamanaka, S., Touhara, K., and Terasawa, H.
  • Journal Title: Biomol. NMR Assign. Volume: 7
  • Peer Reviewed
• [Remarks] 研究成果の紹介「マウスの性行動を制御するペプチド性フェロモンの立体構造と受容体相互作用機構を解明」
  • URL: http://www.a.u-tokyo.ac.jp/topics/2013/20130509-4.html
• [Remarks] マウスの性行動を制御するペプチド性フェロモンの立体構造と受容体相互作用機構を解明
  • URL: http://www.a.u-tokyo.ac.jp/topics/2013/20130509-4.html