Yuji Kubota Division of Cell Signaling and Molecular Medicine, Institute of Medical Science, The University of Tokyo, JAPAN, JAPAN,
1 protocol

Ko Fujioka Division of Cell Signaling and Molecular Medicine, Institute of Medical Science, The University of Tokyo, JAPAN, JAPAN,
1 protocol

Mutsuhiro Takekawa
  • Faculty, Division of Cell Signaling and Molecular Medicine, Institute of Medical Science, The University of Tokyo, JAPAN, JAPAN,
  • 1 Author merit

Education

M.D., Ph.D., Sapporo Medical University School of Medicine, Japan, 1994

Current position

Professor, Division of Cell Signaling and Molecular Medicine, Institute of Medical Science, The University of Tokyo, Japan

Publications

  1. Arimoto-Matsuzaki K, Saito H and Takekawa M. TIA1 oxidation inhibits stress granule assembly and sensitizes cells to stress-induced apoptosis. Nature Commun. 7: 10252 doi:10.1038/ncomms10252 (2016) 
  2. Ichikawa K, Kubota Y, Nakamura T, Weng JS, Tomida T, Saito H and Takekawa M. MCRIP1, an ERK substrate, mediates ERK-induced gene silencing during epithelial-mesenchymal transition by regulating the co-repressor CtBP. Molecular Cell 58: 35-46 (2015) 
  3. Nakamura T, Saito H and Takekawa M. SAPK pathways and p53 cooperatively regulate PLK4 activity and centrosome integrity under stress. Nature Commun. 4:1775 doi:10.1038/ncomms2752 (2013) 
  4. Kubota Y, O’Grady P, Saito H and Takekawa M. Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation. Nature Cell Biol. 13, 282-291 (2011) 
  5. Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, and Takekawa M. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nature Cell Biol. 10, 1324-1332 (2008) 
  6. Takekawa, M., Tatebayashi, K., and Saito, H. Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases. Molecular Cell 18, 295-306 (2005) 
  7. Takekawa M, Tatebayashi K, Itoh F, Adachi M, Imai K and Saito H. Smad-dependent GADD45β expression mediates delayed activation of p38 MAP kinase by TGF-β. EMBO J. 21, 6473-6482 (2002) 
  8. Takekawa M, Adachi M, Nakahata A, Nakayama I, Itoh F, Tsukuda H, Taya Y and Imai K. p53-inducible Wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation. EMBO J., 19, 6517-6526 (2000) 
  9. Takekawa M and Saito H. A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK. Cell 95, 521-530 (1998) 
  10. Takekawa M, Maeda T and Saito H. Protein phosphatase 2Cα inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J. 17, 4744-4752 (1998) 
  11. Takekawa M, Posas F and Saito H. A human homolog of the yeast Ssk2/Ssk22 MAP kinase kinase kinase, MTK1, mediates stress-induced activation of the p38 and JNK pathways. EMBO J. 16, 4973-4982 (1997) 
  12. Maeda T, Takekawa M and Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 269, 554-558 (1995)
1 Protocol published
Wheat Germ Agglutinin (WGA)-SDS-PAGE: A Novel Method for the Detection of O-GlcNAc-modified Proteins by Lectin Affinity Gel Electrophoresis
Authors:  Ko Fujioka, Yuji Kubota and Mutsuhiro Takekawa, date: 12/05/2018, view: 126, Q&A: 0
Diverse cytoplasmic and nuclear proteins dynamically change their molecular functions by O-linked β-N-acetylglucosamine (O-GlcNAc) modification on serine and/or threonine residues. Evaluation of the O-GlcNAcylation level of a specific protein, ...
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