Understanding protein folding in the endoplasmic reticulum (ER) and how cells prevent the exit of non-native polypeptides from this compartment is of fundamental interest. Learning about the processes involved should eventually permit the development of strategies to enhance the production of therapeutic proteins. It is also clear that through aberrant protein folding the ER is closely connected to a number of serious human diseases. So, the topic of ER quality control appeals to a broad spectrum of the life science community, including cell biologists, biochemists, biotechnologists, and medical doctors. In writing our paper we aimed at describing the general mechanisms underlying ER quality control, and at presenting the most interesting recent developments in the field.

My interest in ER chaperones and protein folding started during my Ph.D. studies. In my postdoctoral work, I concentrated on molecular studies of the calnexin/calreticulin system for glycoprotein folding in the ER, and quickly also gained an interest in the cell biology of ER quality control. Currently, my group is mostly focusing on the process of disulfide-bond formation in the ER.