GO TOP

Field

Molecular and Chemical Life Science :
Multilevel Biomolecular Structure and Dynamics

Research

JAPANESE
Professor INABA Kenji
Campus Katahira campus
Laboratory Structural Biology
Tel +81-22-217-5604
E-mail kenji.inaba.a1＠tohoku.ac.jp
Website http://www.tagen.tohoku.ac.jp/labo/inaba/

I was born and grew up in Kyoto. In research, I am passionate and strict, but otherwise I am an open-minded and mild-mannered person. I am happiest when I can pioneer new research fields together with young people in Tohoku.

Career
1993 Graduated from Department of Chemistry, Faculty of Science, Kyoto University
1998 Doctoral program, Graduate School of Engineering, Kyoto University
1998 - 2000 Post-doctoral Fellow, U.K. Medical Research Council
2000 - 2001 Post-doctoral Fellow, Institute for Virus Research, Kyoto University
2001 - 2005 Researcher, JST PRESTO (Sakigake 21)
2005 - 2006 Researcher, JST CREST
2006 - 2011 Specially Appointed Associate Professor, Medical Institute of Bioregulation, Kyushu University
2011 - 2013 Associate Professor, Medical Institute of Bioregulation, Kyushu University
Apr. 2013 - present Professor, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
Selected Publications
  1. Han, Ba Bui, Watanabe, S., Nomura, N., Liu, K., Uemura, T., Inoue, M., Tsutsumi, A., Fujita, H., Kinoshita, K. Kato, Y., Iwata, S., Kikkawa, M., and Inaba, K.* “Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus” Nature Communications 14, 4770 (2023)
  2. Amagai, Y., Yamada, M., Kowada, T., Watanabe, T., Du, Y., Liu, R., Naramoto, S., Watanabe, S., Kyozuka, J., Anelli, T., Tempio, T., Sitia, R., Mizukami, S. and Inaba, K.* “Zinc homeostasis governed by Golgi-resident ZnT family members regulates ERp44-dependent proteostasis at the ER-Golgi interface. Nature Communications 14, 2683 (2023)
  3. Chen, Z., Watanabe, S., Hashida, H., Inoue, M., Daigaku, Y., Kikkawa, M., and Inaba, K.* “Cryo-EM structures of human SPCA1a reveal the mechanism of Ca2+/Mn2+ transport into the Golgi apparatus; Science Advances 9, eadd9742 (2023)
  4. Zhang, Y., Kobayashi, C., Cai, X., Watanabe, S., Tsutsumi, A., Kikkawa, M., Sugita, Y. and Inaba, K.* “Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle; Cell Reports 41, 111760 (2022)
  5. Zhang, Y., Watanabe, S., Tsutsumi, A., Kadokura, H., Kikkawa, M. and Inaba, K.* “Cryo-EM analysis provides new mechanistic insight into ATP binding to Ca2+-ATPase SERCA2b” EMBO Journal 40, e108482 (2021)
  6. Zhang. Y., Inoue, M., Tsutsumi, A., Watanabe, S., Nishizawa, T., Nagata, K., Kikkawa, M. and Inaba, K.* “Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail” Science Advances 6, eabb0147 (2020)
  7. Kadokura, H., Dazai, Y., Fukuda, Y., Hirai, N., Nakamura, O., and Inaba, K. “Observing the nonvectorial yet cotranslational folding of a multidomain protein, LDL receptor, in the ER of mammalian cells” Proc. Natl. Acad. Sci. USA. 117, 16401-16408 (2020)
  8. Okumura, M.*, Noi, K., Kanemura, S., Kinoshita, M., Saio, T., Inoue, Y., Hikima, T., Akiyama, S., Ogura, T.* and Inaba, K.* “Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding” Nature Chemical Biology 15, 499-509 (2019)
  9. Watanabe S., Amagai Y., Sannino S., Tempio T., Anelli T., Harayama M., Masui S., Sorrentino I., Yamada M., Sitia R*, and Inaba K*. “Zinc regulates ERp44-dependent protein quality control in the early secretory pathway.” Nature Communications, 10, 603 (2019)
  10. Inoue, M., Sakuta, N., Watanabe, S., Zhang, Y., Yoshikaie, K., Tanaka, Y., Ushioda, R., Kato, Y., Takagi, J., Tsukazaki, T., Nagata, K. and Inaba, K.* “Structural basis of sarco/endoplasmic reticulum Ca2+-ATPase 2b regulation via transmembrane helix interplay” Cell Reports, 27, 1221-1230 (2019)
  11. Watanabe, S., Harayama, M., Kanemura, S., Sitia, R. and Inaba, K.* “Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface” Proc. Natl. Acad. Sci. USA. 114, 3224-3232 (2017)
  12. Maegawa, K., Watanabe, S., Noi, K., Okumura, M., Amagai, Y., Inoue, M., Ushioda, R., Nagata, K., Ogura, T. and Inaba, K.* “The highly dynamic nature of ERdj5 is key to efficient　elimination of aberrant protein oligomers through ER-associated degradation” Structure, 25, 846-857(2017)
  13. Arai, K., Takei, T., Okumura, M., Watanabe, S., Amagai, Y., Asahina, Y., Moroder, L., Hojo, H.*, Inaba, K.* and Iwaoka, M.* “Preparation of selenoinsulin as a long-lasting insulin analog” Angewandte Chemie 56, 5522-5526 (2017)
  14. Vavassori, S., Cortini, M., Masui, S. Sannino, S., Anelli, T., Caserta, I. R., Fagioli, C., Fornili, A., Mossuto, M. F., Degano, M, Inaba, K. and Sitia, R.* “A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly” Molecular Cell 50, 783-792 (2013)
  15. Hagiwara, M., Maegawa, K., Suzuki, M. †, Ushioda, R., Araki, K., Matsimoto, Y., Hoseki, J., Nagata, K.* and Inaba, K.* “Structural basis of an ERAD pathway mediated by the ER-resident disulfide reductasse ERdj5” Molecular Cell 41, 432-444 (2011)
  16. Inaba, K.*, Masui, S., Iida, H. Vavassori, S., Sitia, R. and Suzuki, M. “Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI” EMBO Journal 29, 3330-3343 (2010)
  17. Inaba, K.*, Murakami, S., Nakagawa, A., Iida, H., Kinjo, M., Ito, K. and Suzuki, M. “Dynamic nature of disulfide bond formation catalysts revealed by crystal structures of DsbB” EMBO Journal 28, 779-791 (2009)
  18. Inaba, K.*, Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K. and Ito, K.* “Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation” Cell 127, 789-801 (2006)
  19. Inaba, K., Takahashi, Y. -H., Ito, K. and Hayashi, S. “Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB” Proc. Natl. Acad. Sci. USA. 103, 287-292 (2006)
  20. Inaba, K. and Ito, K. “Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade” EMBO Journal 21, 2646-2654 (2002)
 
Activities in Academic Societies

Protein Science Society of Japan, the Japanese Biochemical Society, the Molecular Biology Society of Japan, the Biophysical Society of Japan, Japan Society for Cell Biology
Teaching

Advanced Lecture on Biomolecular Sciences, Advanced Biochemistry, Advanced Lecture on Metals Biology I

Recent Activities

Disulfide bonds formed between two cysteine residues are known to play an important role in folding and functional regulation of proteins. Proteins endowed with disulfide bonds include immunoglobulins, MHC molecules, and defensin, which serve as the basis of the immune system; and hormones such as insulin and growth factor. We make full use of structural biology, biochemistry, proteomics, and cell biology techniques in the pursuit of thoroughly elucidating molecular mechanisms and new functional roles of disulfide bond formation and cleavage systems (networks) in cells. In particular, we have recently been conducting research focused on the protein quality control system in the endoplasmic reticulum of human cells. It has been widely reported that the failure of this system causes problems such as diabetes and neurodegenerative diseases like Alzheimer's and Parkinson's, and therefore I believe that our basic research is of much medical importance as well.

Message to Students

Do you hate to lose? Are you thinking about making a living through research? Are you interested in understanding biological phenomena at the molecular level? If you answer “yes” to all of the above, then let us research together. Achieving significant research results requires sense, insatiable enthusiasm, and just a little bit of luck. I am seeking tenacious individuals for my laboratory.

Research