GO TOP

Field

Molecular and Chemical Life Science :
Multilevel Biomolecular Structure and Dynamics

Research

Assistant Professor WATANABE Satoshi
Campus Katahira campus
Laboratory Structural Biology
Tel +81-22-217-5605
E-mail stwata@tagen.tohoku.ac.jp
Website http://www.tagen.tohoku.ac.jp/labo/inaba/
Career
2001 Graduated from Department of Science, Faculty of Science, Kyoto University
2007 Doctor of Science, Kyoto University
2006 Research Fellow, Graduate School of Science, Kyoto University
2007 Postdoctoral Fellow, RIKEN Harima
2007 - 2013 Postdoctoral Fellow, Graduate School of Science, Kyoto University
2013 - present Assistant Professor, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
Selected Publications
 
  1. Watanabe S*, Amagai Y*, Sannino S*, Tempio T, Anelli T, Harayama M, Masui S, Sorrentino I, Yamada M, Sitia R, Inaba K. (*equal contribution)
    Zinc regulates ERp44-dependent protein quality control in the early secretory pathway
    Nat Commun. 2019 Feb 5;10(1):603
  2. Kwon S*, Watanabe S*, Nishitani Y*, Kawashima T, Kanai T., Atomi H., and Miki K (*equal contribution)
    Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA
    Proc. Natl. Acad. Sci. USA, 2018 115 (27) 7045-705
  3. Watanabe S, Harayama M, Kanemura S, Sitia R, 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 U S A. 2017 Apr 18;114(16):E3224-E3232
  4. Maegawa KI, Watanabe S, Noi K, Okumura M, Amagai Y, Inoue M, Ushioda R, Nagata K, Ogura T, 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).
  5. Arai K, Takei T, Okumura M, Watanabe S, Amagai Y, Asahina Y, Moroder L, Hojo H, Inaba K, Iwaoka M.
    Preparation of Selenoinsulin as a Long-Lasting Insulin Analogue
    Angew Chem Int Ed Engl. 2017 May 8;56(20):5522-5526. doi: 10.1002/anie.201701654
  6. Ushioda R, Miyamoto A, Inoue M, Watanabe S, Okumura M, Maegawa KI, Uegaki K, Fujii S, Fukuda Y, Umitsu M, Takagi J, Inaba K, Mikoshiba K, Nagata K.
    “Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by ERdj5"
    Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6055-E6063
  7. Watanabe S, Kawashima T, Nishitani Y, Kanai T, Wada T, Inaba K, Atomi H, Imanaka T, Miki K
    Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.
    Proc Natl Acad Sci U S A. 2015 Jun 3;112(25):7701-6.
  8. Tominaga T, Watanabe S, Matsumi R, Atomi H, Imanaka T, Miki K.
    Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.
    Proc Natl Acad Sci U S A. 110(51):20485-90 (2013)
  9. Watanabe S, Matsumi R, Atomi H, Imanaka T, Miki K.
    “Crystal structures of the HypCD complex and the HypCDE ternary complex: transient intermediate complexes during [NiFe] hydrogenase maturation”
    Structure 20, 2124-2137, 2012
  10. Watanabe S, Kita A, Kobayashi K, Miki K
    "Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA"
    Proc Natl Acad Sci U S A, 105, 4121-6 (2008)
  11. Watanabe S, Matsumi R, Arai T, Atomi H, Imanaka T, Miki K
    "Crystal structures of [NiFe] hydrogenase maturation proteins, HypC, HypD, and HypE: insights into the cyanation reaction by thiol redox signaling"
    Molecular Cell, 27, 29-40 (2007)
Activities in Academic Societies

Protein Science Society of Japan, the Crystallographic Society of Japan, the Japanese Biochemical Society, the Biophysical Society of Japan

Recent Activities

In order to fully understand the functions of proteins, it is necessary to observe their three-dimensional structures at atomic resolution. X-ray crystallography is one of the most powerful techniques for elucidating protein structures. Currently, I am studying calcium ion control mechanisms in the endoplasmic reticulum and the maturation mechanisms of metalloproteins. In particular, I’m interested in the structures of protein-proteins complexes that are transiently formed in cells. I aim to elucidate how proteins function cooperatively on the basis of the atomic structures of these complexes.

Message to Students

I hope that you will experience the fun and excitement of scientific research through studies in our laboratory. You can develop fundamental knowledge and skills, which will help you in any field.