Taste substance binding elicits conformational change of taste receptor T1r heterodimer extracellular domains

Eriko Nango, Shuji Akiyama, Saori Maki-Yonekura, Yuji Ashikawa, Yuko Kusakabe, Elena Krayukhina, Takahiro Maruno, Susumu Uchiyama, Nipawan Nuemket, Koji Yonekura, Madoka Shimizu, Nanako Atsumi, Norihisa Yasui, Takaaki Hikima, Masaki Yamamoto, Yuji Kobayashi, Atsuko Yamashita

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Sweet and umami tastes are perceived by T1r taste receptors in oral cavity. T1rs are class C G-protein coupled receptors (GPCRs), and the extracellular ligand binding domains (LBDs) of T1r1/T1r3 and T1r2/T1r3 heterodimers are responsible for binding of chemical substances eliciting umami or sweet taste. However, molecular analyses of T1r have been hampered due to the difficulties in recombinant expression and protein purification, and thus little is known about mechanisms for taste perception. Here we show the first molecular view of reception of a taste substance by a taste receptor, where the binding of the taste substance elicits a different conformational state of T1r2/T1r3 LBD heterodimer. Electron microscopy has showed a characteristic dimeric structure. Förster resonance energy transfer and X-ray solution scattering have revealed the transition of the dimerization manner of the ligand binding domains, from a widely spread to compactly organized state upon taste substance binding, which may correspond to distinct receptor functional states.

Original languageEnglish
Article number25745
JournalScientific Reports
Volume6
DOIs
Publication statusPublished - May 10 2016

    Fingerprint

ASJC Scopus subject areas

  • General

Cite this

Nango, E., Akiyama, S., Maki-Yonekura, S., Ashikawa, Y., Kusakabe, Y., Krayukhina, E., Maruno, T., Uchiyama, S., Nuemket, N., Yonekura, K., Shimizu, M., Atsumi, N., Yasui, N., Hikima, T., Yamamoto, M., Kobayashi, Y., & Yamashita, A. (2016). Taste substance binding elicits conformational change of taste receptor T1r heterodimer extracellular domains. Scientific Reports, 6, [25745]. https://doi.org/10.1038/srep25745