Nobuko Hosokawa

Summary

Affiliation: Kyoto University
Country: Japan

Publications

  1. doi request reprint The role of MRH domain-containing lectins in ERAD
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Glycobiology 20:651-60. 2010
  2. doi request reprint EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Glycobiology 20:567-75. 2010
  3. pmc Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
    J Biol Chem 283:20914-24. 2008
  4. ncbi request reprint Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Saitama 332 0012, Japan
    Biochem Biophys Res Commun 362:626-32. 2007
  5. pmc Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    J Biol Chem 284:17061-8. 2009
  6. doi request reprint Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant
    Tsutomu Fujimori
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
    FEBS J 280:1563-75. 2013
  7. pmc Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
    Daisuke Morito
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Mol Biol Cell 19:1328-36. 2008
  8. ncbi request reprint Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    J Biol Chem 278:26287-94. 2003
  9. ncbi request reprint EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Genes Cells 11:465-76. 2006
  10. pmc SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates
    Yasutaka Iida
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, 53 Kawahara cho, Shogoin, Sakyo ku, Kyoto 606 8397, Japan
    J Biol Chem 286:16929-39. 2011

Collaborators

Detail Information

Publications18

  1. doi request reprint The role of MRH domain-containing lectins in ERAD
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Glycobiology 20:651-60. 2010
    ..M7A has since been demonstrated to be a degradation signal in both yeast and mammals...
  2. doi request reprint EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Glycobiology 20:567-75. 2010
    ..Based on this observation, we conclude that EDEM1 activity trims mannose from the C branch of N-glycans in vivo...
  3. pmc Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
    J Biol Chem 283:20914-24. 2008
    ....
  4. ncbi request reprint Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Saitama 332 0012, Japan
    Biochem Biophys Res Commun 362:626-32. 2007
    ..Although transfected NHK is primarily localized in the ER, some NHK also co-localizes with Golgi markers, suggesting that mannose trimming by Golgi alpha1,2-mannosidases can also contribute to NHK degradation...
  5. pmc Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    J Biol Chem 284:17061-8. 2009
    ..Thus, we propose a model for mannose trimming and the requirement for hOS-9 lectin activity in glycoprotein ERAD in which N-glycans lacking the terminal mannose from the C branch are recognized by hOS-9 and targeted for degradation...
  6. doi request reprint Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant
    Tsutomu Fujimori
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
    FEBS J 280:1563-75. 2013
    ..Therefore, we propose that XTP3-B recognizes M9 glycans on unfolded polypeptides, thereby acting as a negative regulator of ERAD, and also protects newly synthesized immature polypeptides from premature degradation...
  7. pmc Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
    Daisuke Morito
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Mol Biol Cell 19:1328-36. 2008
    ..Our data demonstrates that gp78 cooperates with RMA1 with E4-like activity in the ERAD of CFTRDeltaF508...
  8. ncbi request reprint Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    J Biol Chem 278:26287-94. 2003
    ....
  9. ncbi request reprint EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Genes Cells 11:465-76. 2006
    ..These results indicate that EDEM may maintain the retrotranslocation competence of NHK by inhibiting aggregation so that unstable misfolded proteins can be accommodated by the dislocon for ERAD...
  10. pmc SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates
    Yasutaka Iida
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, 53 Kawahara cho, Shogoin, Sakyo ku, Kyoto 606 8397, Japan
    J Biol Chem 286:16929-39. 2011
    ..These results indicate that the regulation of the stability and assembly of the HRD1-SEL1L complex is critical to optimize the degradation kinetics of ERAD substrates...
  11. ncbi request reprint EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming
    Kazuyoshi Hirao
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan, CREST, JST, Saitama 332 0012, Japan
    J Biol Chem 281:9650-8. 2006
    ..These results show that EDEM3 has alpha1,2-mannosidase activity in vivo, suggesting that the mechanism whereby EDEM3 accelerates glycoprotein ERAD is different from that of EDEM...
  12. ncbi request reprint EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    Yukako Oda
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    Science 299:1394-7. 2003
    ..Overexpression of EDEM accelerated ERAD by promoting the release of terminally misfolded proteins from calnexin. Thus, EDEM appeared to function in the ERAD pathway by accepting substrates from calnexin...
  13. pmc Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation
    Koji Nagasawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606 8397, Japan
    EMBO Rep 8:483-9. 2007
    ..Thus, the TRAP complex induced by the unfolded protein response pathway might discriminate ERAD substrates from correctly folded substrates, accelerating degradation...
  14. doi request reprint Mannose 6-phosphate receptor homology domain-containing lectins in mammalian endoplasmic reticulum-associated degradation
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
    Methods Enzymol 480:181-97. 2010
    ..We also discuss the structure and function of OS-9 and XTP3-B, and the effect of these lectins on ERAD...
  15. ncbi request reprint [ER quality control and ERAD]
    Nobuko Hosokawa
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, 53 Kawara cho, Shogoin, Sakyo ku, Kyoto 606 8397, Japan
    Seikagaku 75:512-9. 2003
  16. doi request reprint Targeted disruption of Hsp110/105 gene protects against ischemic stress
    Junji Nakamura
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Graduate School of Biostudies, Kyoto University, Shogoin, Kyoto, Japan
    Stroke 39:2853-9. 2008
    ..To study the physiological role of this protein in vivo, we generated hsp110/105 knockout (KO) mice and investigate the effect of reduced Hsp110/105 levels on focal cerebral ischemia...
  17. pmc Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells
    Yasuhiro Matsuoka
    Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Sakyo ku, Kyoto 606 8397, Japan
    Mol Biol Cell 15:4467-75. 2004
    ..These results indicate for the first time that Hsp47 is required for the molecular maturation of type IV collagen and suggest that misfolded type IV collagen causes abnormal morphology of embryoid bodies...
  18. ncbi request reprint A time-dependent phase shift in the mammalian unfolded protein response
    Hiderou Yoshida
    Graduate School of Biostudies, Kyoto University, Kyoto 606 8304, Japan
    Dev Cell 4:265-71. 2003
    ....