Protein aggregation is a process where misfolded proteins aggregate to form insoluble
These aggregates are marked for proteasomal degradation and clearance from the cell by the ubiquitin-proteasome pathway. Inefficient clearing of the aggregated proteins may lead to deleterious cellular outcomes. Indeed, protein aggregation is a hallmark of several neurodegenerative disorders including Alzheimer’s disease, Parkinson’s disease, and Prion diseases. Whether protein aggregation plays a role in the pathophysiology of cancer is not well established. A recent report suggested that tumor suppressor (TP53) mutations may lead to aggregation of TP53 oligomers and chemotherapy resistance in neuroblastoma. The team’s recent in vitro data suggests that FBW7 - an important tumor suppressor - may undergo aggregation upon self-ubiquitylation. Whether the FBW7 protein aggregation contributes to cancer is not known. This project will study the protein aggregation properties of tumor suppressor FBW7 and test the possibility of whether FBW7 protein is aggregated in human cancers.
QAR 30,000 to 60,000 for one year.