フォールディングセンサー酵素UDP-グルコース

DOI Web Site 被引用文献3件 参考文献27件
  • Izumi Masayuki
    Japan Science and Technology Agency (JST), ERATO, Ito Glycotrilogy Project Department of Chemistry, Graduate School of Science, Osaka University
  • Kiuchi Tatsuto
    Department of Chemistry, Graduate School of Science, Osaka University
  • Ito Yukishige
    RIKEN Advanced Science Institute Japan Science and Technology Agency (JST), ERATO, Ito Glycotrilogy Project
  • Kajihara Yasuhiro
    Japan Science and Technology Agency (JST), ERATO, Ito Glycotrilogy Project Department of Chemistry, Graduate School of Science, Osaka University

書誌事項

タイトル別名
  • Misfolded Glycoproteins as Probes for Analysis of Folding Sensor Enzyme UDP-Glucose
  • Glycoprotein Glucosyltransferase
  • 糖タンパク質グルコース転移酵素の機能解明のためのプローブとなる変性糖タンパク質

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抄録

Glycoprotein quality control system exists in the endoplasmic reticulum and discriminates and excludes misfolded glycoproteins. The key component of this system is UDP-glucose : glycoprotein glucosyltransferase (UGGT), which serves as a folding sensor as it can only monoglucosylate misfolded glycoproteins. Monoglucosylation serves as a tag for refolding assisted by lectin chaperones calnexin/calreticulin. To elucidate the recognition mechanism of misfolding by UGGT, various sophisticated misfolded glycoprotein models have been reported. Variety of model glycoproteins can be prepared by biological approaches although those are usually heterogeneous in both glycan and protein structures. Recently, we introduced a chemical approach for the synthesis of homogeneous misfolded glycoprotein. Chemical method can provide small glycoproteins but with homogeneous glycan and with intentionally manipulated protein 3D-structure. In this review, both chemical and biological approaches for the preparation of misfolded glycoprotein probes are discussed, which will give us an ability to gain further insights into the glycoprotein quality control system.

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