Hidetaka Kosako

Summary

Affiliation: The University of Tokushima
Country: Japan

Publications

  1. ncbi Quantitative phosphoproteomics strategies for understanding protein kinase-mediated signal transduction pathways
    Hidetaka Kosako
    Division of Disease Proteomics, Institute for Enzyme Research, The University of Tokushima, 3 18 15 Kuramoto cho, Tokushima 770 8503, Japan
    Expert Rev Proteomics 8:81-94. 2011
  2. ncbi Phosphorylation of nucleoporins: signal transduction-mediated regulation of their interaction with nuclear transport receptors
    Hidetaka Kosako
    Division of Disease Proteomics Institute for Enzyme Research The University of Tokushima Tokushima, Japan
    Nucleus 1:309-13. 2010
  3. ncbi Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
    Hidetaka Kosako
    Division of Cellular Proteomics BML, Institute of Medical Science, The University of Tokyo, Tokyo, Japan
    Nat Struct Mol Biol 16:1026-35. 2009
  4. ncbi Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1
    Yutaka Harita
    Division of Cellular Proteomics BML and Department of Oncology, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    J Biol Chem 284:8951-62. 2009
  5. ncbi Extracellular signal-regulated kinase/mitogen-activated protein kinase regulates actin organization and cell motility by phosphorylating the actin cross-linking protein EPLIN
    Mei Ying Han
    Division of Cellular Proteomics BML, The Institute of Medical Science, The University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    Mol Cell Biol 27:8190-204. 2007
  6. ncbi Identification of protein kinase substrates by proteomic approaches
    Seisuke Hattori
    Division of Biochemistry, School of Pharmaceutical Science, Kitasato University, 5 9 1 Shirokane, Minato ku, Tokyo, Japan
    Expert Rev Proteomics 5:497-505. 2008
  7. ncbi Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2
    Yutaka Harita
    Division of Cellular Proteomics BML, Institute of Medical Science, The University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo, Japan
    J Biol Chem 283:9177-86. 2008
  8. ncbi Purification of phosphoproteins by immobilized metal affinity chromatography and its application to phosphoproteome analysis
    Mitsuyo Machida
    Division of Cellular Proteomics BML, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 6639, Japan
    FEBS J 274:1576-87. 2007
  9. ncbi Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate
    Koji Ueda
    Division of Cellular Proteomics, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    J Biol Chem 279:41815-21. 2004
  10. ncbi Global analysis of dynamic changes in lipid raft proteins during T-cell activation
    Michimoto Kobayashi
    Division of Cellular Proteomics BML, Institute of Medical Science, University of Tokyo, Minato ku, Tokyo, Japan
    Electrophoresis 28:2035-43. 2007

Collaborators

Detail Information

Publications10

  1. ncbi Quantitative phosphoproteomics strategies for understanding protein kinase-mediated signal transduction pathways
    Hidetaka Kosako
    Division of Disease Proteomics, Institute for Enzyme Research, The University of Tokushima, 3 18 15 Kuramoto cho, Tokushima 770 8503, Japan
    Expert Rev Proteomics 8:81-94. 2011
    ..In this article, we present an overview of several strategies for quantitative phosphoproteomics and discuss how phosphoproteomic analysis can help to elucidate signaling pathways that regulate various cellular processes...
  2. ncbi Phosphorylation of nucleoporins: signal transduction-mediated regulation of their interaction with nuclear transport receptors
    Hidetaka Kosako
    Division of Disease Proteomics Institute for Enzyme Research The University of Tokushima Tokushima, Japan
    Nucleus 1:309-13. 2010
    ..An understanding of the effects of signaling pathways on nucleocytoplasmic transport machinery is only beginning to emerge...
  3. ncbi Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport
    Hidetaka Kosako
    Division of Cellular Proteomics BML, Institute of Medical Science, The University of Tokyo, Tokyo, Japan
    Nat Struct Mol Biol 16:1026-35. 2009
    ..Thus, we propose that ERK phosphorylates various nucleoporins to regulate nucleocytoplasmic transport...
  4. ncbi Phosphorylation of Nephrin Triggers Ca2+ Signaling by Recruitment and Activation of Phospholipase C-{gamma}1
    Yutaka Harita
    Division of Cellular Proteomics BML and Department of Oncology, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    J Biol Chem 284:8951-62. 2009
    ..Given the profound effect of PLC-gamma in diverse cellular functions, regulation of the Ca(2+) signaling by Nephrin may be important in modulating the glomerular filtration barrier function...
  5. ncbi Extracellular signal-regulated kinase/mitogen-activated protein kinase regulates actin organization and cell motility by phosphorylating the actin cross-linking protein EPLIN
    Mei Ying Han
    Division of Cellular Proteomics BML, The Institute of Medical Science, The University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    Mol Cell Biol 27:8190-204. 2007
    ..We propose that ERK-mediated phosphorylation of EPLIN contributes to actin filament reorganization and enhanced cell motility...
  6. ncbi Identification of protein kinase substrates by proteomic approaches
    Seisuke Hattori
    Division of Biochemistry, School of Pharmaceutical Science, Kitasato University, 5 9 1 Shirokane, Minato ku, Tokyo, Japan
    Expert Rev Proteomics 5:497-505. 2008
    ..The final section contains an expert opinion on the current strategies and the issues we are going to challenge in the next 5 years...
  7. ncbi Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2
    Yutaka Harita
    Division of Cellular Proteomics BML, Institute of Medical Science, The University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo, Japan
    J Biol Chem 283:9177-86. 2008
    ..Thus, SFK orchestrates a wide spectrum of protein-protein interactions and intracellular signaling networks at SD through tyrosine phosphorylation...
  8. ncbi Purification of phosphoproteins by immobilized metal affinity chromatography and its application to phosphoproteome analysis
    Mitsuyo Machida
    Division of Cellular Proteomics BML, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 6639, Japan
    FEBS J 274:1576-87. 2007
    ..These results demonstrate the efficacy of phosphoprotein enrichment by IMAC and suggest that this procedure will be of general use in phosphoproteome research...
  9. ncbi Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate
    Koji Ueda
    Division of Cellular Proteomics, Institute of Medical Science, University of Tokyo, 4 6 1 Shirokanedai, Minato ku, Tokyo 108 8639, Japan
    J Biol Chem 279:41815-21. 2004
    ..We confirmed that MAPKAP kinase 2 is also required for phosphorylation of BAG2 in vivo. Thus, p38 MAPK-MAPKAP kinase 2-BAG2 phosphorylation cascade may be a novel signaling pathway for response to extracellular stresses...
  10. ncbi Global analysis of dynamic changes in lipid raft proteins during T-cell activation
    Michimoto Kobayashi
    Division of Cellular Proteomics BML, Institute of Medical Science, University of Tokyo, Minato ku, Tokyo, Japan
    Electrophoresis 28:2035-43. 2007
    ..We also demonstrated that these proteins assembled at the T-cell/APC interface. These results indicate the efficacy of our system to systematically analyze dynamics of lipid raft proteins during extracellular stimulation...