2019 年 31 巻 181 号 p. SE95-SE97
Asparagine (N)-linked glycosylation occurs on most secretory and membrane proteins synthesized in the endoplasmic reticulum (ER), which functions to modulate protein folding, degradation and intracellular trafficking. However, the regulatory mechanisms underlying N-linked glycosylation remain largely elusive, hindering our integrative understanding of the physiological and pathological functions of this posttranslational modification. In this article, I will introduce recent advances on our understanding of regulation of N-linked glycosylation and a newly discovered inhibitor of N-linked glycosylation reaction.