Research Topics
Genomes and Genes
| Nobuko HosokawaSummaryAffiliation: Kyoto University Country: Japan Publications
| Collaborators
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Detail Information
Publications
The role of MRH domain-containing lectins in ERADNobuko 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...- EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycansNobuko 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... 
Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPNobuko Hosokawa
Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto, Japan
J Biol Chem 283:20914-24. 2008....
Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidasesNobuko 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...- Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansNobuko 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... - Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variantTsutomu 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... - Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508Daisuke 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... - Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase INobuko 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.... - EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsinNobuko 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... - SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesYasutaka 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... - EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimmingKazuyoshi 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... - EDEM as an acceptor of terminally misfolded glycoproteins released from calnexinYukako 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... - Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradationKoji 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... - Mannose 6-phosphate receptor homology domain-containing lectins in mammalian endoplasmic reticulum-associated degradationNobuko 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... - [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 - Targeted disruption of Hsp110/105 gene protects against ischemic stressJunji 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... - Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cellsYasuhiro 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... - A time-dependent phase shift in the mammalian unfolded protein responseHiderou Yoshida
Graduate School of Biostudies, Kyoto University, Kyoto 606 8304, Japan
Dev Cell 4:265-71. 2003....