Updated on 2024/10/01

写真a

 
SHIMIZU Kouhei
 
Organization
Graduate School of Medicine Department of Basic Medical Science Lecturer
School of Medicine Department of Medical Science
Title
Lecturer
Affiliation
Institute of Medicine
Homepage
http://osaka-cu-1seika.umin.jp/index.html

Position

  • Graduate School of Medicine Department of Basic Medical Science 

    Lecturer  2024.10 - Now

  • Graduate School of Medicine Department of Basic Medical Science 

    Assistant Professor  2022.04 - 2024.09

  • School of Medicine Department of Medical Science 

    Lecturer  2024.10 - Now

  • School of Medicine Department of Medical Science 

    Assistant Professor  2022.04 - 2024.09

Degree

  • 博士（工学） （ Ehime University ）

Research Areas

  • Life Science / Molecular biology

  • Nanotechnology/Materials / Chemical biology

  • Life Science / Tumor biology

  • Life Science / Immunology

  • Life Science / Pathological biochemistry

Research Interests

  • ユビキチン

  • 翻訳後修飾

  • 炎症

  • 免疫

  • タンパク質分解

  • 創薬

  • 細胞死

  • がん

Research Career

  • ユビキチン修飾系と疾患発症メカニズム

    2014 - Now 

Professional Memberships

  • 日本生化学会

      Domestic

  • 日本分子生物学会

      Domestic

Awards

  • 1st Prize Poster Presentation

    Kouhei Shimizu

    2023.08   The 3rd Japan and Australia Meeting on Cell Death (JAM2023)   LUBAC and its associated ubiquitin ligase generate heterotypic ubiquitin chains to inhibit necroptosis

  • ベストプレゼンテーション賞

    清水 康平

    2023.07   日本Cell Death学会   新規LUBAC結合E3による複合型ユビキチン鎖形成を介したネクロプトーシスの制御

  • 2021年度 Teacher of the Year

    清水 康平

    2022.03   大阪市立大学医学部  

Job Career (off-campus)

  • 東北大学   大学院歯学研究科 先端再生医学研究センター   助教

    2017.01 - 2019.09

  • Harvard Medical School   Department of Pathology, Beth Israel Deaconess Medical Center   日本学術振興会海外特別研究員

    2017.01 - 2017.05

  • Harvard Medical School   Department of Pathology, Beth Israel Deaconess Medical Center   Research Fellow

    2014.10 - 2016.12

  • 愛媛大学   プロテオサイエンスセンター   研究員

    2014.04 - 2014.09

  • 愛媛大学   プロテオサイエンスセンター   日本学術振興会特別研究員(PD)

    2013.10 - 2014.03

  • 愛媛大学   大学院理工学研究科   日本学術振興会特別研究員(DC1)

    2011.04 - 2013.09

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Papers

  • Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1. Reviewed

    Daisuke Oikawa, Kouhei Shimizu, Fuminori Tokunaga

    Antioxidants (Basel, Switzerland)   12 ( 2 )   2023.02（ ISSN:2076-3921 ）

    　More details

    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Protein ubiquitination, which is catalyzed by ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin ligases, is a crucial post-translational modification to regulate numerous cellular functions in a spatio-temporal-specific manner. The human genome encodes ~100 deubiquitinating enzymes (DUBs), which antagonistically regulate the ubiquitin system. OTUD1, an ovarian tumor protease (OTU) family DUB, has an N-terminal-disordered alanine-, proline-, glycine-rich region (APGR), a catalytic OTU domain, and a ubiquitin-interacting motif (UIM). OTUD1 preferentially hydrolyzes lysine-63-linked ubiquitin chains in vitro; however, recent studies indicate that OTUD1 cleaves various ubiquitin linkages, and is involved in the regulation of multiple cellular functions. Thus, OTUD1 predominantly functions as a tumor suppressor by targeting p53, SMAD7, PTEN, AKT, IREB2, YAP, MCL1, and AIF. Furthermore, OTUD1 regulates antiviral signaling, innate and acquired immune responses, and cell death pathways. Similar to Nrf2, OTUD1 contains a KEAP1-binding ETGE motif in its APGR and regulates the reactive oxygen species (ROS)-mediated oxidative stress response and cell death. Importantly, in addition to its association with various cancers, including multiple myeloma, OTUD1 is involved in acute graft-versus-host disease and autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and ulcerative colitis. Thus, OTUD1 is an important DUB as a therapeutic target for a variety of diseases.

    DOI： 10.3390/antiox12020350

    PubMed

  • Involvement of heterologous ubiquitination including linear ubiquitination in Alzheimer's disease and amyotrophic lateral sclerosis. Reviewed

    Yusuke Sato, Seigo Terawaki, Daisuke Oikawa, Kouhei Shimizu, Yoshinori Okina, Hidefumi Ito, Fuminori Tokunaga

    Frontiers in molecular biosciences   10   1089213 - 1089213   2023.01（ ISSN:2296-889X ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    In neurodegenerative diseases such as Alzheimer's disease (AD) and amyotrophic lateral sclerosis (ALS), the progressive accumulation of ubiquitin-positive cytoplasmic inclusions leads to proteinopathy and neurodegeneration. Along with the seven types of Lys-linked ubiquitin chains, the linear ubiquitin chain assembly complex (LUBAC)-mediated Met1-linked linear ubiquitin chain, which activates the canonical NF-κB pathway, is also involved in cytoplasmic inclusions of tau in AD and TAR DNA-binding protein 43 in ALS. Post-translational modifications, including heterologous ubiquitination, affect proteasomal and autophagic degradation, inflammatory responses, and neurodegeneration. Single nucleotide polymorphisms (SNPs) in SHARPIN and RBCK1 (which encodes HOIL-1L), components of LUBAC, were recently identified as genetic risk factors of AD. A structural biological simulation suggested that most of the SHARPIN SNPs that cause an amino acid replacement affect the structure and function of SHARPIN. Thus, the aberrant LUBAC activity is related to AD. Protein ubiquitination and ubiquitin-binding proteins, such as ubiquilin 2 and NEMO, facilitate liquid-liquid phase separation (LLPS), and linear ubiquitination seems to promote efficient LLPS. Therefore, the development of therapeutic approaches that target ubiquitination, such as proteolysis-targeting chimeras (PROTACs) and inhibitors of ubiquitin ligases, including LUBAC, is expected to be an additional effective strategy to treat neurodegenerative diseases.

    DOI： 10.3389/fmolb.2023.1089213

    PubMed

  • OTUD1 deubiquitinase regulates NF-κB- and KEAP1-mediated inflammatory responses and reactive oxygen species-associated cell death pathways Reviewed

    Daisuke Oikawa, Min Gi, Hidetaka Kosako, Kouhei Shimizu, Hirotaka Takahashi, Masayuki Shiota, Shuhei Hosomi, Keidai Komakura, Hideki Wanibuchi, Daisuke Tsuruta, Tatsuya Sawasaki, Fuminori Tokunaga

    Cell Death & Disease   13 ( 8 )   694   2022.08（ eISSN:2041-4889 ）

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    Publishing type：Research paper (scientific journal)  

    Abstract

    Deubiquitinating enzymes (DUBs) regulate numerous cellular functions by removing ubiquitin modifications. We examined the effects of 88 human DUBs on linear ubiquitin chain assembly complex (LUBAC)-induced NF-κB activation, and identified OTUD1 as a potent suppressor. OTUD1 regulates the canonical NF-κB pathway by hydrolyzing K63-linked ubiquitin chains from NF-κB signaling factors, including LUBAC. OTUD1 negatively regulates the canonical NF-κB activation, apoptosis, and necroptosis, whereas OTUD1 upregulates the interferon (IFN) antiviral pathway. Mass spectrometric analysis showed that OTUD1 binds KEAP1, and the N-terminal intrinsically disordered region of OTUD1, which contains an ETGE motif, is indispensable for the KEAP1-binding. Indeed, OTUD1 is involved in the KEAP1-mediated antioxidant response and reactive oxygen species (ROS)-induced cell death, oxeiptosis. In Otud1<sup>−/−</sup>-mice, inflammation, oxidative damage, and cell death were enhanced in inflammatory bowel disease, acute hepatitis, and sepsis models. Thus, OTUD1 is a crucial regulator for the inflammatory, innate immune, and oxidative stress responses and ROS-associated cell death pathways.

    DOI： 10.1038/s41419-022-05145-5

    PubMed

    Other URL： https://www.nature.com/articles/s41419-022-05145-5

  • Interplay between protein acetylation and ubiquitination controls MCL1 protein stability. Reviewed

    Shimizu K, Gi M, Suzuki S, North BJ, Watahiki A, Fukumoto S, Asara JM, Tokunaga F, Wei W, Inuzuka H

    Cell reports   37 ( 6 )   109988 - 109988   2021.11

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    Publishing type：Research paper (scientific journal)  

    The anti-apoptotic myeloid cell leukemia 1 (MCL1) protein belongs to the pro-survival BCL2 family and is frequently amplified or elevated in human cancers. MCL1 is highly unstable, with its stability being regulated by phosphorylation and ubiquitination. Here, we identify acetylation as another critical post-translational modification regulating MCL1 protein stability. We demonstrate that the lysine acetyltransferase p300 targets MCL1 at K40 for acetylation, which is counteracted by the deacetylase sirtuin 3 (SIRT3). Mechanistically, acetylation enhances MCL1 interaction with USP9X, resulting in deubiquitination and subsequent MCL1 stabilization. Therefore, ectopic expression of acetylation-mimetic MCL1 promotes apoptosis evasion of cancer cells, enhances colony formation potential, and facilitates xenografted tumor progression. We further demonstrate that elevated MCL1 acetylation sensitizes multiple cancer cells to pharmacological inhibition of USP9X. These findings reveal that acetylation of MCL1 is a critical post-translational modification enhancing its oncogenic function and provide a rationale for developing innovative therapeutic strategies for MCL1-dependent tumors.

    DOI： 10.1016/j.celrep.2021.109988

    PubMed

  • Inhibition of CK1ε potentiates the therapeutic efficacy of CDK4/6 inhibitor in breast cancer. Reviewed

    Dang F, Nie L, Zhou J, Shimizu K, Chu C, Wu Z, Fassl A, Ke S, Wang Y, Zhang J, Zhang T, Tu Z, Inuzuka H, Sicinski P, Bass AJ, Wei W

    Nature communications   12 ( 1 )   5386 - 5386   2021.09

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    Publishing type：Research paper (scientific journal)  

    Although inhibitors targeting CDK4/6 kinases (CDK4/6i) have shown promising clinical prospect in treating ER+/HER2- breast cancers, acquired drug resistance is frequently observed and mechanistic knowledge is needed to harness their full clinical potential. Here, we report that inhibition of CDK4/6 promotes βTrCP1-mediated ubiquitination and proteasomal degradation of RB1, and facilitates SP1-mediated CDK6 transcriptional activation. Intriguingly, suppression of CK1ε not only efficiently prevents RB1 from degradation, but also prevents CDK4/6i-induced CDK6 upregulation by modulating SP1 protein stability, thereby enhancing CDK4/6i efficacy and overcoming resistance to CDK4/6i in vitro. Using xenograft and PDX models, we further demonstrate that combined inhibition of CK1ε and CDK4/6 results in marked suppression of tumor growth in vivo. Altogether, these results uncover the molecular mechanisms by which CDK4/6i treatment alters RB1 and CDK6 protein abundance, thereby driving the acquisition of CDK4/6i resistance. Importantly, we identify CK1ε as an effective target for potentiating the therapeutic efficacy of CDK4/6 inhibitors.

    DOI： 10.1038/s41467-021-25700-6

    PubMed

  • Th2 cell-derived histamine is involved in nasal Th2 infiltration in mice. Reviewed

    Iwasaki N, Terawaki S, Shimizu K, Oikawa D, Sakamoto H, Sunami K, Tokunaga F

    Inflammation research   70 ( 5 )   539 - 541   2021.05（ ISSN:1023-3830 ）

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    Publishing type：Research paper (scientific journal)  

    OBJECTIVE: Histamine derived from mast cells and basophils plays important roles in inducing allergic symptoms. Although T cells also produce histamine, the involvement of the histamine produced from T cells has remained enigmatic. We sought to reveal the roles of T helper 2 (Th2) cell-derived histamine in nasal allergic disorders. METHODS: The histamine production from Th2 cells was measured by EIA. The mRNA expression of histidine decarboxylase (HDC) was measured by real-time PCR. To investigate the roles of Th2 cell-derived histamine in vivo, we analyzed an antigen-specific Th2 cell transfer mouse model. RESULTS: Th2 cells produced histamine by T cell receptor stimulation, and these properties were specific for Th2 cells, but not Th1 cells and naïve CD4 T cells. The histamine produced from Th2 cells was involved in the infiltrations of Th2 cells in response to antigen exposure. CONCLUSION: These results suggest that Th2 cell-derived histamine play important roles in nasal allergic disorders.

    DOI： 10.1007/s00011-021-01458-x

    PubMed

  • Th2 cells and macrophages cooperatively induce allergic inflammation through histamine signaling. Reviewed

    Iwasaki N, Terawaki S, Shimizu K, Oikawa D, Sakamoto H, Sunami K, Tokunaga F

    PloS one   16 ( 3 )   e0248158   2021

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1371/journal.pone.0248158

    PubMed

  • Phosphorylation-dependent osterix degradation negatively regulates osteoblast differentiation. Reviewed

    Hoshikawa S, Shimizu K, Watahiki A, Chiba M, Saito K, Wei W, Fukumoto S, Inuzuka H

    FASEB journal   34 ( 11 )   14930 - 14945   2020.11（ ISSN:0892-6638 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1096/fj.202001340R

    PubMed

  • Lipin-2 degradation elicits a proinflammatory gene signature in macrophages. Reviewed

    Watahiki A, Shimizu K, Hoshikawa S, Chiba M, Kitamura H, Egusa H, Fukumoto S, Inuzuka H

    Biochemical and biophysical research communications   2020.01（ ISSN:0006-291X ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.bbrc.2020.01.119

    PubMed

  • The E3 ubiquitin ligase MIB2 enhances inflammation by degrading the deubiquitinating enzyme CYLD. Reviewed

    Uematsu A, Kido K, Takahashi H, Takahashi C, Yanagihara Y, Saeki N, Yoshida S, Maekawa M, Honda M, Kai T, Shimizu K, Higashiyama S, Imai Y, Tokunaga F, Sawasaki T

    The Journal of biological chemistry   294 ( 38 )   14135 - 14148   2019.09（ ISSN:0021-9258 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1074/jbc.RA119.010119

    PubMed

  • Physiological functions of FBW7 in cancer and metabolism. Reviewed

    Shimizu K, Nihira NT, Inuzuka H, Wei W

    Cellular signalling   46   15 - 22   2018.06（ ISSN:0898-6568 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.cellsig.2018.02.009

    PubMed

  • NOTCH2 Hajdu-Cheney Mutations Escape SCFFBW7-Dependent Proteolysis to Promote Osteoporosis. Reviewed

    Fukushima H, Shimizu K, Watahiki A, Hoshikawa S, Kosho T, Oba D, Sakano S, Arakaki M, Yamada A, Nagashima K, Okabe K, Fukumoto S, Jimi E, Bigas A, Nakayama KI, Nakayama K, Aoki Y, Wei W, Inuzuka H

    Molecular cell   68 ( 4 )   645 - 658.e5   2017.11（ ISSN:1097-2765 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.molcel.2017.10.018

    PubMed

  • Prostate cancer-associated SPOP mutations confer resistance to BET inhibitors through stabilization of BRD4. Reviewed

    Dai X, Gan W, Li X, Wang S, Zhang W, Huang L, Liu S, Zhong Q, Guo J, Zhang J, Chen T, Shimizu K, Beca F, Blattner M, Vasudevan D, Buckley DL, Qi J, Buser L, Liu P, Inuzuka H, Beck AH, Wang L, Wild PJ, Garraway LA, Rubin MA, Barbieri CE, Wong KK, Muthuswamy SK, Huang J, Chen Y, Bradner JE, Wei W

    Nature medicine   23 ( 9 )   1063 - 1071   2017.09（ ISSN:1078-8956 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/nm.4378

    PubMed

  • G1 cyclins link proliferation, pluripotency and differentiation of embryonic stem cells. Reviewed

    Liu L, Michowski W, Inuzuka H, Shimizu K, Nihira NT, Chick JM, Li N, Geng Y, Meng AY, Ordureau A, Kołodziejczyk A, Ligon KL, Bronson RT, Polyak K, Harper JW, Gygi SP, Wei W, Sicinski P

    Nature cell biology   19 ( 3 )   177 - 188   2017.03（ ISSN:1465-7392 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/ncb3474

    PubMed

  • Nutrient-induced FNIP degradation by SCFβ-TRCP regulates FLCN complex localization and promotes renal cancer progression. Reviewed

    Nagashima K, Fukushima H, Shimizu K, Yamada A, Hidaka M, Hasumi H, Ikebe T, Fukumoto S, Okabe K, Inuzuka H

    Oncotarget   8 ( 6 )   9947 - 9960   2017.02

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.18632/oncotarget.14221

    PubMed

  • Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function. Reviewed

    Nihira NT, Ogura K, Shimizu K, North BJ, Zhang J, Gao D, Inuzuka H, Wei W

    Science signaling   10 ( 466 )   2017.02（ ISSN:1945-0877 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1126/scisignal.aai8026

    PubMed

  • The SCFβ-TRCP E3 ubiquitin ligase complex targets Lipin1 for ubiquitination and degradation to promote hepatic lipogenesis. Reviewed

    Shimizu K, Fukushima H, Ogura K, Lien EC, Nihira NT, Zhang J, North BJ, Guo A, Nagashima K, Nakagawa T, Hoshikawa S, Watahiki A, Okabe K, Yamada A, Toker A, Asara JM, Fukumoto S, Nakayama KI, Nakayama K, Inuzuka H, Wei W

    Science signaling   10 ( 460 )   2017.01（ ISSN:1945-0877 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1126/scisignal.aah4117

    PubMed

  • The apoptotic initiator caspase-8: its functional ubiquity and genetic diversity during animal evolution. Reviewed

    Sakamaki K, Shimizu K, Iwata H, Imai K, Satou Y, Funayama N, Nozaki M, Yajima M, Nishimura O, Higuchi M, Chiba K, Yoshimoto M, Kimura H, Gracey AY, Shimizu T, Tomii K, Gotoh O, Akasaka K, Sawasaki T, Miller DJ

    Molecular biology and evolution   31 ( 12 )   3282 - 3301   2014.12（ ISSN:0737-4038 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1093/molbev/msu260

    PubMed

  • Pctaire1/Cdk16 promotes skeletal myogenesis by inducing myoblast migration and fusion. Reviewed

    Shimizu K, Uematsu A, Imai Y, Sawasaki T

    FEBS letters   588 ( 17 )   3030 - 3037   2014.08（ ISSN:0014-5793 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.febslet.2014.05.060

    PubMed

  • Nek5, a novel substrate for caspase-3, promotes skeletal muscle differentiation by up-regulating caspase activity. Reviewed

    Shimizu K, Sawasaki T

    FEBS letters   587 ( 14 )   2219 - 2225   2013.07（ ISSN:0014-5793 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.febslet.2013.05.049

    PubMed

  • Stress-inducible caspase substrate TRB3 promotes nuclear translocation of procaspase-3. Reviewed

    Shimizu K, Takahama S, Endo Y, Sawasaki T

    PloS one   7 ( 8 )   e42721   2012

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1371/journal.pone.0042721

    PubMed

  • Caspase-8 cleavage of the interleukin-21 (IL-21) receptor is a negative feedback regulator of IL-21 signaling. Reviewed

    Akagi T, Shimizu K, Takahama S, Iwasaki T, Sakamaki K, Endo Y, Sawasaki T

    FEBS letters   585 ( 12 )   1835 - 1840   2011.06（ ISSN:0014-5793 ）

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.febslet.2011.04.031

    PubMed

  • Characterization of a caspase-3-substrate kinome using an N- and C-terminally tagged protein kinase library produced by a cell-free system. Reviewed

    Tadokoro D, Takahama S, Shimizu K, Hayashi S, Endo Y, Sawasaki T

    Cell death & disease   1   e89   2010.10

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/cddis.2010.65

    PubMed

  • Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins. Reviewed

    Matsunaga S, Matsuoka K, Shimizu K, Endo Y, Sawasaki T

    BMC biotechnology   10   42   2010.06

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1186/1472-6750-10-42

    PubMed

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MISC

  • Involvement of a novel LUBAC-associated protein on the regulation of cell death pathways Reviewed

    清水康平, GI Min, LINH Tran, 及川大輔, 小迫英尊, 高橋宏隆, 澤崎達也, 徳永文稔

    日本分子生物学会年会プログラム・要旨集(Web)   45th   2022

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Grant-in-Aid for Scientific Research

  • 複雑化ユビキチン修飾による細胞生死制御の細胞・個体レベルでの解析と病態との関連

    Grant-in-Aid for Scientific Research(B)  2026

  • 複合型ユビキチン鎖を標的とした筋萎縮性側索硬化症の病態解明と創薬シーズの開拓

    挑戦的研究(開拓)  2025

  • 複雑化ユビキチン修飾による細胞生死制御の細胞・個体レベルでの解析と病態との関連

    Grant-in-Aid for Scientific Research(B)  2025

  • 新規RING型E3によるSkp2プロテオスタシス制御の破綻と発がん機構の解明

    Grant-in-Aid for Scientific Research(C)  2024

  • 複雑化ユビキチン修飾による細胞生死制御の細胞・個体レベルでの解析と病態との関連

    Grant-in-Aid for Scientific Research(B)  2024

  • 複合型ユビキチン鎖を標的とした筋萎縮性側索硬化症の病態解明と創薬シーズの開拓

    挑戦的研究(開拓)  2024

  • 新規RING型E3によるSkp2プロテオスタシス制御の破綻と発がん機構の解明

    Grant-in-Aid for Scientific Research(C)  2022.04

  • 複合型ユビキチン鎖を標的とした筋萎縮性側索硬化症の病態解明と創薬シーズの開拓

    Grant-in-Aid for Challenging Research (Pioneering)/(Exploratory)  2022

  • LUBACを介した生体防御応答を制御する新規ユビキチン化酵素の解析

    Grant-in-Aid for Early-Career Scientists  2020.04

  • 歯周組織再生を目指した効率的な抗炎症療法の開発

    Grant-in-Aid for Scientific Research(B)  2019.04

  • Establishment of a method for improving the efficiency of stem cell differentiation using a protein knockdown strategy

    Grant-in-Aid for Challenging Research (Pioneering)/(Exploratory)  2018.06

  • Molecular mechanisms of p75NTR modulation in the regeneration of pulp sensory function

    Grant-in-Aid for Challenging Research (Pioneering)/(Exploratory)  2018.06

  • 腫瘍性タンパク質Skp2の量的制御を司る幹細胞腫瘍化抑制機構の包括的解析

    Grant-in-Aid for Research Activity Start-up  2017.08

  • Identification of proteolytic signaling pathways regulating reprogramming during iPS cell generation

    Grant-in-Aid for Challenging Research (Pioneering)/(Exploratory)  2016.04

  • 切断プロファイリング解析によるカスパーゼ依存シグナル伝達ネットワーク機構の解明

    Grant-in-Aid for JSPS Fellows  2011

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Contract research

  • リニアユビキチンコードが制御する生体防御応答機構の解析と応用

    国立研究開発法人科学技術振興機構  戦略的創造研究推進事業（ACT-X)　加速フェーズ  2024.04

  • リニアユビキチンコードが制御する生体防御応答機構の解析と応用

    国立研究開発法人科学技術振興機構  戦略的創造研究推進事業（ACT-X)  2021.10

Incentive donations / subsidies

  • がんにおけるMCL1過剰発現機構の解明とその治療応用

    公益財団法人武田科学振興財団  2019.10

  • がん遺伝子産物Skp2の分解を介した新規がん抑制機構の解明

    日本学術振興会  2017.01

  • がん遺伝子産物Skp2の分解を介したがん抑制機構の解明

    上原記念生命科学財団  2016.01

  • Skp2の分解を誘導する新規E3リガーゼの同定及びその分解に依存するがん抑制機構の解析

    内藤記念科学振興財団  2014.10

Other subsidies, etc.

  • ユビキチン修飾系による細胞内抗炎症機構の解明と治療応用

    大学  2020.04

Charge of on-campus class subject

  • 遺伝医学

    2023   Intensive lecture   Undergraduate

  • 医学研究推進コースII （遺伝子コース）

    2023   Practical Training   Undergraduate

  • 医学研究推進コース

    2023   Intensive lecture   Undergraduate

  • 細胞生物学

    2023   Weekly class   Undergraduate

  • 修業実習

    2023   Practical Training   Undergraduate

  • 遺伝と遺伝子コース

    2023   Weekly class   Undergraduate

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Other

  • Job Career

    2019.10 - Now