| 日本語 (Japanese) | |||
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Graduate School of Life Sciences, Tohoku University |
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Field
Research
| Campus | Katahira campus |
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| Laboratory |
Structural Biology
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| Tel | +81-22-217-5605 |
| hiroshi.kadokura.b3＠tohoku.ac.jp | |
| Website | http://www.tagen.tohoku.ac.jp/labo/inaba/ |
https://scholar.google.co.jp/citations?user=qQjpVogAAAAJ&hl=ja
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.
| Career |
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| 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) |
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| Activities in Academic Societies |
Japan Society for Bioscience, Biotechnology, and Agrochemistry; Japan Bioindustry Association; the Japanese Biochemical Society |
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| Teaching |
Biochemistry IIB (AMC), Advanced molecular and chemical biology seminar III |
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.