Cell and Developmental biology


Organelle Biogenesis and Homeostasis

Pedro Carvalho
Ombretta Foresti, Montserrat Serra, Gabriel E Mora
Alexandra Grippa, Annamaria Ruggiano, Lisa Johnsen, Victoria Rodríguez , Nivedita Natarajan (started September)
Laura Buxó


Figure 1: A model depicting quality control of ER membrane proteins by spatially segregated ERAD complexes

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

Selected Publications

Foresti O, Rodriguez-Vaello V, Funaya C, Carvalho P.
“Quality control of inner nuclear membrane proteins by the Asi complex.”
Science, 346(6210):751-5 (2014).

Stein A, Ruggiano A, Carvalho P, Rapoport TA.
“Key steps in ERAD of luminal ER proteins reconstituted with purified components.” Cell, 158(6):1375-88 (2014).

Ruggiano A, Foresti O, Carvalho P.
“Quality control: ER-associated degradation: protein quality control and beyond.”
J Cell Biol, 204(6):869-79 (2014). Review.