2019 Volume 31 Issue 181 Pages SE69-SE70
N-glycan acts as quality control tag for determination of intracellular glycoprotein fates. I have demonstrated the structural basis for N-glycan-dependent determination of glycoprotein fates at atomic level by using several biophysical methods including X-ray crystallography. In 2012, I received a JSCR young science award entitled “Structural biology study of intracellular lectins involved in glycoprotein transport and degradation.” In recent years, I have focused on ER glycoprotein folding system, i.e., calnexin/calreticulin cycle, and successfully determined 3D structures of ER glucosidase II (GII) and UDP-glucose:glycoprotein glucosyltransferase (UGGT), which are respectively responsible for glucose trimming and attachment, providing structural insights into ER quality control mediated by glucose tagging.
