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Biomolecular Networks Laboratories Research Group of Lipid Biosignals (Prof. Okamoto)
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Biomolecular Networks Laboratories
Research Group of Lipid Biosignals
Biomolecular Dynamics Group
Developmental Biology Group
Chromosome Replication Group

Integrated Biology Laboratories
Laboratory of Genetics
Pathology Division
KOKORO-Biology Group
Cellular Biology Group

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Developmental Genetics Group
Human Cell Biology Group
Medicine and Pathophysiology Group

Neuroscience Laboratories
Visual Neuroscience Group
Developmental and Functional Neuroscience Group
Cognitive Neuroscience Group
Cellular and Molecular Neurobiology Group
Synaptic Plasticity Group

Biophysical Dynamics Laboratories
Physiological Laboratory
Nonequilibrium Physics Group
Functional Proteomics Group
Nano-Biophotonics Group

Biomedical Engineering Laboratories
Systems Neuroscience Group
Department of Molecular Genetics
Laboratory of Intercellular Communications
Laboratory of Stem Cell Research
Laboratory of Protein Informatics
Laboratory of Biocatalysis Science

Collaborative institutes
Laboratory of Immune Regulation Chugai Pharmaceutical CO.,LTD.
Optical Nano Device Group
OMRON Corporation

Lab. Members

Kazuhiro IWAI Professor
Hiromasa Tojo Associate Professor
Shin-Ichi SAKATA Postdoctoral Fellow
Ryo UETA Postdoctoral Fellow
Yukiko TAKEDA Graduate Student D1



  Publications

Iwai痴 group
  1. Miyauchi, Y., Kato, M., Tokunaga, F., and Iwai, K. The COP9/signalosome increases the efficiency of pVHL ubiquitin ligase卜ediated hypoxia inducible factor-? ubiquitination. J. Biol. Chem. In press.


  2. Shabek, N., Iwai, K., and Ciechanover, A. Ubiquitin is degraded by the ubiquitin system as a monomer and as part of its conjugated target. Biochem Biophys Res Commun. 363: 425-431, 2007.


  3. Ueta, R., Fujiwara, N., Iwai, K. (corresponding author) and Yamaguchi-Iwai, Y. Mechanism underlying the iron-dependent nuclear export of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae. Mol. Biol. Cell 18:2980-2990, 2007.


  4. Sakata, E., Yamaguchi, Y., Miyauchi, Y., Iwai, K., Chiba, T., Saeki, Y., Matsuda, N., Tanaka, K. and Kato, K. Direct interactions between Nedd8 and ubiquitin E2 conjugating enzymes contribute to up-regulation of cullin-based E3 ligase activity. Nature Struct. Mol. Biol. 14:167-168, 2007.


  5. Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, K., Sano, S. Tokunaga, F., Tanaka, K. and Iwai, K. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J. 25: 48774887. 2006.


  6. Nakamura, M., Tokunaga, F., Sakata , S.-I. and Iwai, K. Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex (LUBAC). Biochem. Biophys. Res. Commun. 351:340-347, 2006.


  7. Lorick, K., Yang, Y., Jensen, J., Iwai, K. and Weissman, A.M. Studies of the ubiquitin proteasome system. Units 15.9 Sections 1-12. Current Protocols in Cell Biology Bonifacino J, Dasso M, Lippincott-Schwartz J, Harford J, Yamada K, Bonafacino J, eds. John Wiley and Sons; 2006.


  8. Ishikawa, H., Kato, M., Hori, H., Ishimori, K., Kirisako, T., Tokunaga, F. and Iwai, K. Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Molecular Cell 19:171-181, 2005.


  9. Megumi, Y., Miyauchi, Y., Sakurai, H., Nobeyama, H., Lorick, K, Nakamura, E., Chiba, T., Tanaka, K., Weissman, A. M., Kirisako, T., Ogawa, O. and Iwai, K. Multiple roles of Rbx1 in the VBC-Cul2 ubiquitin ligase complex. Genes to Cells, 10:679-691, 2005.


  10. Mizushima, T., Hirao, T., Yoshida, Y., Lee, S.J., Chiba, T., Iwai, K., Yamaguchi, Y., Kato, K., Tsukihara, T. and Tanaka, K. Structural basis of sugar-recognizing ubiquitin ligase. Nat. Struct. Mol. Biol. 11: 365-70, 2004.


  11. Meyron-Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre-Wilson, H., Grinberg, A., Love, P. and Rouault, T. A. Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis. EMBO J. 23:386-395, 2004.


  12. Yamanaka, K., Ishikawa, H., Megumi, Y., Tokunaga, F., Kanie, M., Rouault, T.A., Morishima, I., Minato, N., Ishimori, K. and Iwai, K. Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2. Nature Cell Biol. 5:336-340, 2003.


  13. Ishida, D., Kometani, K., Yang, H., Kakugawa, K., Masuda, K., Iwai, K., Suzuki, M., Itohara, S., Nakahata, T., Hiai, H., Kawamoto, H., Hattori, M. and Minato, N. Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1-deficient mice. Cancer Cell. 4:55-65, 2003.


  14. Yoshida, Y., Chiba, T., Tokunaga, F., Kawasaki, H., Iwai, K., Suzuki, T., Ito, Y., Matsuoka, K., Yoshida, M., Tanaka, K. and Tai, T. E3 ubiquitin-ligase that recognizes sugar chains. Nature 418: 438-442, 2002.


  15. LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., Switzer III, R., Grinberg, A., Love, P., Tresser N. and Rouault, T. Targeted deletion of iron regulatory protein 2 causes iron overload and neurodegenerative disease in mice. Nature Genet. 27:209-214, 2001.


  16. Kamura, T., Sato, S., Iwai, K., Czyzyk-Krzeska, M., Conaway, R.C. and Conaway, J.W. Activation of HIF1? ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc. Natl. Acad. Sci. USA. 97:10430-10435, 2000.


  17. Shimura, H., Hattori, N., Kubo, S-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K. and Suzuki, T. Familial Parkinson's disease gene product, Parkin, is a ubiquitin-protein ligase. Nature Genet. 25:302-305, 2000.


  18. Iwai, K., Yamanaka, K., Kamura, T., Minato, N., Conaway, R. C., Conaway, J. W., Klausner, R. D. and Pause, A. Identification of the von Hippel-Lindau tumor suppressor protein as part of an active E3 ubiquitin ligase complex. Proc. Natl. Acad. Sci, USA 96:12436-12441, 1999.


  19. Levkowitz, G., Waterman, H., Ettenberg, S. A., Katz, M., Tysgankov, A. Y., Alroy, I., Lavi, S., Iwai, K., Reiss, Y., Ciechanover, A., Lipkowitz, S. and Yarden, Y. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Molecular Cell. 4: 1029-1040, 1999.


  20. Yamanaka, K., Minato, N. and Iwai, K. Stabilization of iron regulatory protein 2, IRP2, by aluminum. FEBS Lett. 462:216-220, 1999.


  21. Iwai, K., Drake, S. K., Wehr, N. B., Weissman, A. M., LaVaute, T. M., Minato, N., Klausner, R. D., Levine, R. L. and Rouault, T. A. Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins. Proc. Natl. Acad. Sci. USA 95:4924-4928, 1998.


  22. Iwai, K., Klausner, R.D. and Rouault, T.A. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO. J. 14:5350-5357, 1995.

Tojo痴 Group
  1. Ikushiro, H., Islam, M., Tojo, H., and Hayashi, H., Molecular Characterization of Membrane-Associated Soluble Serine Palmitoyltransferases from Sphingobacterium multivorun, Sphingobacterium spiritivorun and Bdellovibrio stolpii. J. Bactriol. 189, 5749-5761 (2007).


  2. Nagatsuka, Y., Tojo, H., and Hirabayashi, Y. Identification and Analysis of Novel Glycolipids in Vertebrate Brains by HPLC/Mass Spectrometry. Methods Enzymol. 417, 155-167 (2006). .


  3. Tokuoka, K., Nakajima, Y., Hirotsu, K., Miyahara, I., Nishina, Y., Shiga, K., Tamaoki, H., Setoyama, C., Tojo, H., and Miura, R. Three-Dimensional Structure of Rat-Liver Acyl-CoA Oxidase in Complex with Fatty Acid: Insights into Substrate-Recognition and Reactivity toward Molecular Oxygen. J. Biochem. 139, 789–795 (2006)


  4. Kondo, G., Tojo, H., Nakatani, Y., Komazawa, N., Murata, C., Yamagata, K., Maeda, Y., Kinoshita, T., Okabe, M., Taguchi, R., Takeda, J. The Angiotensin-converting Enzyme (ACE) is a GPI-anchored Protein Releasing Factor Crucial for Fertilization. Nature Med. 11, 160-166 (2005)


  5. Nakagawa, M., Yamano, T., Kuroda, K., Nonaka, Y., Tojo, H., and Fujii, S. A cytosolic cytochrome b5-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme. Biochem. Biophys. Res. Commun. 338, 605-609 (2005).


  6. Tojo, H. Properties of an electrospray emitter coated with material of low surface energy. J. Chromatogr. A 1056, 223-228 (2004)


  7. Fujii, K., Nakano, T., Hike, H., Usui, F., Bando, Y., Tojo, H., Nishimura,T. Fully automated online multi-dimensional protein profiling system for complex mixtures. J. Chromatogr. A 1057, 107-113 (2004)


  8. Takagi, S., Tojo, H., Tomita, S., Sano, S., Itami, S., Hara, M., Inoue, S., Horie, K., Kondoh, G., Hosokawa, K., Gonzalez, F.J. and Takeda, J. Alteration of the 4-sphingenine scaffolds of ceramides in keratinocyte-specific Arnt deficient mice affects skin barrier function. J. Clin. Invest. 112, 1372-1382 (2003)


  9. Ito, M., Tchoua, U., Okamoto, M., and Tojo, H. Purification and Properties of a Phospholipase A2/Lipase Preferring Phosphatidic acid, Bis(monoacylglycerol) Phosphate, and Monoacylglycerol from Rat Testis. J. Biol. Chem. 277, 43674-43681, (2002)


  10. Lu, T., Ito, M., Tchoua, U., Takemori, H., Okamoto, M. and Tojo, H. (2001) Identification of essential residues for catalysis of rat intestinal phospholipase B/lipase. Biochemistry, 19, 7133-7139.

  11. Tchoua, U., Ito, M., Okamoto, M., and Tojo, H. (2000) Increased intestinal phospholipase A2 activity catalyzed by phospholipase B/lipase in WBN/Kob rats with pancreatic insufficiency. Biochimica Biophysica Acta, 1487, 255-67.

  12. Takemori, H., Zolotaryov, F.N., Ting, L., Urbain, T., Komatsubara, T., Hatano, O., Okamoto, M., and Tojo, H. (1998)?Identification of functional domains of rat intestinal phospholipase B/lipase. Its cDNA cloning, expression, and tissue distribution. J. Biol. Chem.,273, 2222-2231.

  13. Tojo, H., Ichida, T., and Okamoto, M. (1998)? Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes. J. Biol. Chem., 273, 2214-2221.


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