Molecular and Chemical Life Science :
Multilevel Biomolecular Structure and Dynamics


Associate Professor KADOKURA Hiroshi
Campus Katahira campus
Laboratory Structural Biology
Tel +81-22-217-5605
E-mail hiroshi.kadokura.b3@tohoku.ac.jp
Website http://www.tagen.tohoku.ac.jp/labo/inaba/
Google scholar


In my career, I have had opportunities to work with a variety of people at various locations, including Tokyo, Boston, Ann Arbor, and Nara. I would like to take advantage of these experiences for my works (teaching and researches) in Tohoku University. I would also like to learn a lot from the members of Tohoku University to do good science.

1985 Graduated from Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo
1990 Completion of doctoral course and acquisition of Doctor of Agriculture, Department of Agricultural Chemistry, Graduate School of Agriculture and Life Sciences, University of Tokyo
1990 - 2000 Assistant Professor, Faculty of Agriculture/ Graduate School of Agriculture, University of Tokyo
(1999) (Visiting Assistant Professor, Monbusho Fellowship Program for Japanese Scholars and Researchers to Study Abroad)
2000 - 2002 Visiting Assistant Professor, Harvard Medical School
2002 - 2008 Instructor, Harvard Medical School
2008 - 2013 International Research Fellow/ Post-doctoral Fellow, Graduate School of Biological Sciences, Nara Institute of Science and Technology
2013 to present Associate Professor, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
Selected Publications
Kadokura H*, Dazai Y, Fukuda Y, Hirai N, Nakamura O, 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)

Fujimoto T, Inaba K, Kadokura H.* Methods to identify the substrates of thiol-disulfide oxidoreductases. Protein Sci 28, 30-40 (2019)

Fujimoto T, Nakamura O, Saito M, Tsuru A, Matsumoto M, Kohno K, Inaba K, Kadokura H* Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family member. J Biol Chem 293, 18421-18433 (2018)

Tsuchiya Y, Saito M, Kadokura H, Miyazaki J-I, Tashiro F, Imagawa Y, Iwawaki T, Kohno K.* IRE1-XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells. J Cell Biol 217, 1287-1301 (2018)

Tsuru A, Fujimoto N, Takahashi S, Saito M, Nakamura D, Iwano M, Iwawaki T, Kadokura H, Ron D, Kohno K.* Negative feedback by IRE1β optimizes mucin production in goblet cells. Proc Natl Acad Sci USA 110, 2864-2869 (2013)

Chng SS, Xue M, Garner RA, Kadokura H, Boyd D, Beckwith J, Kahne D* Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export. Science 337, 1665-1668 (2012)

Yanagitani K, Kimata Y, Kadokura H, Kohno K.* Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA. Science 331, 586-589 (2011)

Kadokura H*, Beckwith J* Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell 138, 1164-1173 (2009)

Kadokura H, Tian H, Zander T, Bardwell JCA, Beckwith J.* Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding. Science 303, 534-537 (2004)

Kadokura H*, Katzen F*, Beckwith J.* Protein disulfide bond formation in prokaryotes. Ann Rev Biochem 72, 111-135 (2003)

Kadokura H, Beckwith J.* Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J 21, 2354-2363 (2002)

Kadokura H, Bader M, Tian HP, Bardwell JCA, Beckwith J.* Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Proc Natl Acad Sci USA 97, 10884-10889 (2000)
Activities in Academic Societies

Japan Society for Bioscience, Biotechnology, and Agrochemistry; Japan Bioindustry Association; the Japanese Biochemical Society


Biochemistry IIB (AMC), Advanced molecular and chemical biology seminar III

Recent Activities

Protein disulfide bonds are covalent bridges formed by oxidation of two cysteines. Lack of efficient formation of disulfide bonds in vivo can lead to diseases such as diabetes. Thus, understanding their mechanisms is important also from a practical viewpoint. The formation of disulfide bonds may look as if it is a very simple reaction. However, organisms have evolved elaborate systems to ensure rapid and correct formation of disulfide bonds that occurs within cells. To understand the mechanisms, I mainly use mammalian cells and a variety of techniques, including those from cell biology, chemical genetics, and proteomics.

Message to Students

I would like to develop a variety of methods to observe and understand the reactions that occur within cells. By doing so, let us discover novel factors or mechanisms involved in disulfide bond formation, and share the excitement.