Calnexin /Calreticulin Cycle and Glycoprotein ER-Associated Degradation

In eukaryotic endoplasmic reticulum (ER), Calnexin and/or Calreticulin cycle and glycoprotein ER-associated degradation both serve the same quality-control mechanism for glycoprotein proper configuration, which superintends structural folding process, and makes the unassembled subunits of glycoprotein refold. Misfolded glycoproteins have to be degraded via a mechanism known as glycoprotein ER-associated degradation if they can not be properly folded. However, malfunction in ER resulting from endoplasmic reticulum stress might lead to further disturbances in Calnexin and/or Calreticulin cycle and GERAD, thereafter, those accumulated misfolded glycoproteins in the case of ER stress lead to the dysfunction of the cells and some diseases. An better understanding of Calnexin and/or Calreticulin cycle and GERAD mechanism can help clinicians treat such diseases as viral hepatitis, Parkinson's disease etc.