Tumor Suppressor Fbw7 Protein Aggregation - A Novel Tumorigenic Mechanism In Cancer?
Back to Research PageProtein aggregation is a process where misfolded proteins aggregate to form insoluble
complexes.
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.
Lead Principal Investigator (LPI)
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