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.

Research projects

  • 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