Folding and quality control of proteins in the endoplasmic reticulum

• Research unit: IRB
• Project number: 2000-MM-01

Key words (English)

Cell Biology, Endoplasmic Reticulum, Protein Folding and Quality Control

Short description (English)

The endoplasmic reticulum (ER) is a membrane-enclosed organelle that represents the entry site of newly synthesized proteins in the secretory pathway. The lumen of the ER is filled with resident molecular chaperones and folding factors that assist the maturation of newly synthesized polypeptides. As a rule, newly synthesized proteins can leave the ER and be secreted or targeted to their final destination only if they are properly folded and completely assembled. The protein-production machinery of the ER is subjected to quality control. Proteins that are not folded or that are incompletely assembled are retained in this compartment to be exposed longer to the folding environment. Terminally misfolded products are eventually degraded to avoid display of non-functional proteins that could result detrimental for cell and organism viability.

Project aims (English)

Our interest is to study the synthesis, folding and intracellular transport of viral proteins and of cellular proteins such as the amyloid precursor protein and the beta-secretase, responsible for the degeneration of brain tissue in Alzheimer's disease. A better understanding of the mechanisms underlying protein folding and assembly may lead to new strategies to block the expression of harmful proteins produced by viruses and other infectious agents. Furthermore, by monitoring these processes it may be possible to prevent the formation of protein aggregates as observed in neuro-degenerative diseases.