The endoplasmic reticulum (ER) is the primary site for the biogenesis of membrane and secreted proteins. Folding and maturation of these proteins is an elaborate process, frequently involving a number of posttranslational modifications (like disulphide bonds, glycosylation, lipidation, etc.) and/or assembly into protein complexes. Most of the cellular lipids are also synthesized at the ER. Perturbations in any of these processes often result in ER stress, a hallmark of many diseases such as diabetes, obesity and cancer. Our long-term goal is to understand how these multiple functions of the ER are coordinated and integrated under different physiological conditions.
- Mechanisms of recognition and degradation of misfolded proteins by ERAD
- Identification of novel regulated ERAD substrates
- Regulation of sterol homeostasis by ERAD
- Novel mechanisms of protein quality control in the ER
- Quality control of inner nuclear membrane proteins
- Mechanisms of lipid droplet biogenesis at the ER
- Mechanisms of protein targeting to lipid droplets