Team Director
Reiya Taniguchi
Ph.D.
Laboratory for In situ Structural Biology
[Affiliation has changed to RIKEN Center for Integrated Medical Sciences (IMS) as of April 2025]
LocationYokohama / Central Research Building
E-mailreiya.taniguchi@riken.jp
The intracellular space is a highly complex environment, where diverse macromolecules coexist with multiple cellular organelles in an extremely crowded manner. How individual protein molecules behave under such conditions and how those molecules interact with the surrounding environment to fulfill biological functions remain largely unexplored. Our team is trying to address this fundamental question by visualizing and analyzing protein structures in situ , using cryo-electron tomography. Specifically, we focus on intracellular vesicle trafficking and cargo sorting processes, aiming to understand their molecular basis from a structural perspective.
Selected Publications
Taniguchi R, Orniacki C, Kreysing JP, et al.
Nuclear pores safeguard the integrity of the nuclear envelope
bioRxiv
(2024)
doi: 10.1101/2024.02.05.578890
Xing H, Taniguchi R, Khusainov I, et al.
Translation dynamics in human cells visualized at high resolution reveal cancer drug action.
Science
381(6653), 70-75 (2023)
doi: 10.1126/science.adh1411
Mosalaganti S, Obarska-Kosinska A, Siggel M, et al.
AI-based structure prediction empowers integrative structural analysis of human nuclear pores.
Science
376(6598), eabm9506 (2022)
doi: 10.1126/science.abm9506
Kato T, Kumazaki K, Wada M, et al.
Crystal structure of plant vacuolar iron transporter VIT1.
Nature Plants
5(3), 308-315 (2019)
doi: 10.1038/s41477-019-0367-2
Oda K, Vierock J, Oishi S, et al.
Crystal structure of the red light-activated channelrhodopsin Chrimson.
Nature Communications
9(1), 3949 (2018)
doi: 10.1038/s41467-018-06421-9
Taniguchi R, Inoue A, Sayama M, et al.
Structural insights into ligand recognition by the lysophosphatidic acid receptor LPA6.
Nature
548(7667), 356-360 (2017)
doi: 10.1038/nature23448
Taniguchi R, Kato HE, Font J, et al.
Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin.
Nature Communications
6, 8545 (2015)
doi: 10.1038/ncomms9545
