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Associate Professor
Fumihiko OkumuraBrief personal historyApril 1st, 2019 to presentAssociate professor, laboratory of Biological Chemistry, Department of Food and Health Sciences, International College of Arts and Sciences Fukuoka Women's University October 1st, 2016 to March 31st, 2019 Jr. Associate professor, Group of Molecular and Cell Biology, Graduate School of Science, Nagoya University, Japan April 1st, 2011 to September 31, 2016 Assistant professor, Group of Molecular and Cell Biology, Graduate School of Science, Nagoya University, Japan March 1st, 2008 to March 31st, 2011 Assistant professor, Department of Biochemistry, Graduate School of Medicine, Hokkaido University, Japan April 1st, 2005 to February 13th, 2008 Research associate, The Scripps Research Institute, USA April 1st, 2001 to March 25th, 2005 Graduate student (Ph.D.), Department of Medicine, Kyushu University, Japan April 1st 1999 to March 25th 2001 Graduate student (Master course), Pharmaceutical department, Kyushu University, Japan April 1st 1995 to March 25th 1999 Undergraduate student, Pharmaceutical department, Kobe-gakuin University, Japan DegreesPh.D.Pharmaceutist Research themesRegulation of enzymatic activity by post-translational modificationBrief explanation of researchAmount of protein expression is regulated by "synthesis" and "degradation". Ubiquitin modification (ubiquitylation)-dependent protein degradation is important and failure of this system causes many types of diseases. In contrast, ubiquitin-like protein ISG15 also modifies proteins (ISGylation). So far, the role of ISGylation has not been cleared, but we hypothesize that the ISGylation may activate enzymes. We are going to keep studying both ubiquitylation and ISGylation.Select publication list1.Nakatsukasa, K., Fujisawa, M., Yang, X., Kawarasaki, T., Okumura, F., and Kamura, T. Triacylglycerol lipase Tgl4 is a stable protein and its dephosphorylation is regulated in a cell cycle-dependent manner in Saccharomyces cerevisiae, Biochemical and Biophysical Research Communications 626, 85-91 (2022). 2.Oki, N., Yamada, S., Tanaka, T., Fukui, H., Hatakeyama, S., and Okumura, F. Curcumin partly prevents ISG15 activation via ubiquitin-activating enzyme E1-like protein and decreases ISGylation, Biochemical and Biophysical Research Communications 625, 94-101 (2022). 3.Kusama, K., Suzuki, Y., Kurita, E., Kawarasaki, T., Obara, K., Okumura, F., Kamura, T., and Nakatsukasa, K. Dot6/Tod6 degradation fine-tunes the repression of ribosome biogenesis under nutrient-limited conditions, iScience 25, 103986 (2022). 4.Okumura, F., Oki, N., Fujiki, Y., Ikuta, R., Osaki, K., Hamada, S., Nakatsukasa, K., Hisamoto, N., Hara, T., and Kamura, T. ZSWIM8 is a myogenic protein that partly prevents C2C12 differentiation, Scientific Reports 11, 20880 (2021). Co-corresponding author. 5.Okumura, F., Fujiki, Y., Oki, N., Osaki, K., Nishikimi, A., Fukui, Y., Nakatsukasa, K., and Kamura, T. Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding, iScience 23, 100970 (2020). Co-corresponding author. 6.Okumura, F. and Kamura, T. (2019) Ubiquitin-proteasome-dependent degradation of single-pass transmembrane protein EphB2, Journal of Japanese Biochemical Society 91(5): 681-685. Co-corresponding author. 7.Okumura, F., Joo-Okumura, A., Obara, K., Petersen, A., Nishikimi, A., Fukui, Y., Nakatsukasa, K., and Kamura, T. (2017) Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by EphB2, Molecular Biology of the Cell 28, 3532-3541. Co-corresponding author. 8.Okumura, F., Joo-Okumura, A., Nakatsukasa, K., and Kamura, T. (2017) Hypoxia-inducible factor-2alpha stabilizes the von Hippel-Lindau (VHL) disease suppressor, Myb-related protein 2, PLoS one 12, e0175593. Co-corresponding author. 9.Uematsu, K., Okumura, F., Tonogai, S., Joo-Okumura, A., Alemayehu, D. H., Nishikimi, A., Fukui, Y., Nakatsukasa, K., and Kamura, T. (2016) ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation, Journal of Cell Biology 215, 95-106. Co-first and Co-corresponding author. 10.Okumura, F., Uematsu, K., Byrne, S. D., Hirano, M., Joo-Okumura, A., Nishikimi, A., Shuin, T., Fukui, Y., Nakatsukasa, K., and Kamura, T. (2016) Parallel Regulation of von Hippel-Lindau Disease by pVHL-Mediated Degradation of B-Myb and Hypoxia-Inducible Factor alpha, Molecular and Cellular Biology 36, 1803-1817. Co-corresponding author. 11.Okumura, F., Joo-Okumura, A., Nakatsukasa, K., and Kamura, T. (2016) The role of cullin 5-containing ubiquitin ligases, Cell Division 11, 1. Co-corresponding author. 12.Okumura, F., Okumura, A. J., Uematsu, K., Hatakeyama, S., Zhang, D. E., and Kamura, T. (2013) Activation of double-stranded RNA-activated protein kinase (PKR) by interferon-stimulated gene 15 (ISG15) modification down-regulates protein translation, Journal of Biological Chemistry, 288, 2839-2847. Co-corresponding author. 13.Okumura, F., Okumura, A., Nakatsukasa, K., and Kamura, T. (2013) [Regulation of cellular functions by Elongin BC based E3 ubiquitin ligase], Seikagaku 85, 76-88. Co-corresponding author. 14.Okumura, F., Matsuzaki, M., Nakatsukasa, K., and Kamura, T. (2012) The Role of Elongin BC-Containing Ubiquitin Ligases, Frontiers in Oncology, 2, 10. Co-corresponding author. 15.Okumura, F., Yoshida, K., Liang, F., and Hatakeyama, S. (2011) MDA-9/syntenin interacts with ubiquitin via a novel ubiquitin-binding motif, Molecular and Cellular Biochemistry, 352, 163-172. 16.Okumura, F., Okumura, A. J., Matsumoto, M., Nakayama, K. I., and Hatakeyama, S. (2011) TRIM8 regulates Nanog via Hsp90beta-mediated nuclear translocation of STAT3 in embryonic stem cells, Biochimica et Biophysica Acta, 1813, 1784-1792. 17.Okumura, F., Matsunaga, Y., Katayama, Y., Nakayama, K. I., and Hatakeyama, S. (2010) TRIM8 modulates STAT3 activity through negative regulation of PIAS3, Journal of Cell Science, 123, 2238-2245. 18.Okumura, F., Kameda, H., Ojima, T., and Hatakeyama, S. (2010) Expression of recombinant sea urchin cellulase SnEG54 using mammalian cell lines, Biochemical and Biophysical Research Communications, 395, 352-355. 19.Okumura, F. (2009) [Regulation of immune response by ubiquitin-like molecule ISG15], Seikagaku 81, 223-232. 20.Okumura, F., Lenschow, D. J., and Zhang, D. E. (2008) Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization of ISG15 and contributes to effective ISGylation, Journal of Biological Chemistry, 283, 24484-24488. 21.Okumura, F., Zou, W., and Zhang, D. E. (2007) ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP, Genes and Development, 21, 255-260. 22.Okumura, F., Hatakeyama, S., Matsumoto, M., Kamura, T., and Nakayama, K. I. (2004) Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis, Journal of Biological Chemistry, 279, 53533-53543. Research fieldBiochemistry, Molecular biology.Membership of Academic SocietiesThe Japanese biochemical societyThe molecular biology society of Japan The pharmaceutical society of Japan Funds2022 Yamada science foundation2021 Mishima Kaiun Memorial Foundation 2020 Ichiro Kanehara Foundation 2019 Mochida memorial foundation for medical and pharmaceutical research 2019 Ito chubei foundation 2018-2022 JSPS Grant-in-Aid for Scientific Research (C)
2018 Sumitomo Foundation
2017 Takeda science foundation 2017-2019 JSPS Grant-in-Aid for Scientific Research (B)(shared) 2015-2017 JSPS Grant-in-Aid for Young Scientists (B) 2014 Inamori foundation 2013-2014 JSPS Grant-in-Aid for Young Scientists (B) 2013 Uehara memorial foundation 2013-2015 JSPS Grant-in-Aid for Scientific Research (B)(shared) 2011-2012 JSPS Grant-in-Aid for Scientific Research on Innovative Areas 2010 Akiyama life science foundation 2009-2010 JSPS Grant-in-Aid for challenging Exploratory Research 2009 Senshin medical research foundation 2008 JSPS Grant-in-Aid for Young Scientists (Start-up) Awards2005 The Uehara memorial foundation postdoctoral fellowshipContributions to local societyAnti-infective drug, anti-cancer drug, and regeneration medicine etc.Related field
Keywordsubiquitin, ubiquitin-like molecule ISG15, post-translational modification, protein degradation, interferonTitles of high school lectures"Clearance of cellular protein and disease""Introduction of school of science, Nagoya university" |
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