The University of Tokyo · 생화학·유전·분자생물학
이 교수의 연구실은 세포의 스트레스 반응 메커니즘을 중심으로, 특히 산화 스트레스와 관련된 신호 전달 경로, 예를 들어 p38 및 JNK MAPK 경로의 활성화 메커니즘을 연구하고 있습니다. TIA1 단백질의 산화적 조절, MTK1(또는 MEKK4) 단백질의 이환성 조절 및 산화-환원 반응에 의한 활성화 등 세포 생존과 사멸의 결정적 조절 기전을 규명하고 있습니다. 또한 스트레스 반응과 관련된 단백질의 번역 후 수정, 예를 들어 O-GlcNAc화의 분석 기법 개발에도 기여하고 있습니다.
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Cytoplasmic stress granules (SGs) are multimolecular aggregates of stalled translation pre-initiation complexes that prevent the accumulation of misfolded proteins, and that are formed in response to certain types of stress including ER stress. SG formation contributes to cell survival not only by suppressing translation but also by sequestering some apoptosis regulatory factors. Because cells can be exposed to various stresses simultaneously in vivo, the regulation of SG assembly under multiple
The mitogen-activated protein kinase (MAPK) module, composed of a MAPK, a MAPK kinase (MAPKK), and a MAPKK kinase (MAPKKK), is a cellular signaling device that is conserved throughout the eukaryotic world. In mammalian cells, various extracellular stresses activate two major subfamilies of MAPKs, namely, the Jun N-terminal kinases and the p38/stress-activated MAPK (SAPK). MTK1 (also called MEKK4) is a stress-responsive MAPKKK that is bound to and activated by the stress-inducible GADD45 family o
Cells respond to oxidative stress by inducing intracellular signaling, including stress-activated p38 and JNK MAPK (SAPK) pathways, but the underlying mechanisms remain unclear. Here, we report that the MAP three kinase 1 (MTK1) SAPK kinase kinase (SAPKKK) functions as an oxidative-stress sensor that perceives the cellular redox state and transduces it into SAPK signaling. Following oxidative stress, MTK1 is rapidly oxidized and gradually reduced at evolutionarily conserved cysteine residues. Th
Mammalian cells are frequently exposed to a variety of environmental stresses, such as ultraviolet rays, ionizing radiation, genotoxins, heat shock, and oxidative stress. In coping with the barrage of these and other stresses, multi-cellular eukaryotic organisms have developed a strategy as to how damaged cells will respond to stresses. In general, if the intensity of the damage is moderate, the cell will seek to repair the damage. If, however, the damage to a cell is too severe to be repaired,
Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc) occurs selectively on serine and/or threonine residues of cytoplasmic and nuclear proteins, and dynamically regulates their molecular functions. Since conventional strategies to evaluate the O-GlcNAcylation level of a specific protein require time-consuming steps, the development of a rapid and easy method for the detection and quantification of an O-GlcNAcylated protein has been a challenging issue. Here, we describe
We report a case of hypereosinophilic syndrome (HES) with marked eosinophilia (59.7%) and mononeuritis multiplex (upper limbs and buttocks). Necrosis of the finger tips was the primary manifestation which simultaneously occurred on both sides. These clinical manifestations were improved dramatically by subsequent steroid therapy. Interestingly, an elevation of serum tumor necrosis factor (TNF) was observed. These findings suggest that TNF may play a role in the etiology of necrosis of the finger
