Research from the Federal University of Rio de Janeiro (UFRJ) and the National Institute of Science and Technology for Structural Biology and Bioimaging (INBEB) in Brazil has uncovered a critical mechanism by which mutations in the p53 protein—a key tumor suppressor known as the "guardian of the genome"—turn other proteins into cancer-promoting agents. The study, led by Dr. Jerson Lima Silva, offers fresh insights into a process that plays a pivotal role in the development and progression of many cancers.
The findings were recently published in Communications Chemistry . p53 is central to the body's defense against cancer , tasked with regulating the cell cycle and triggering the death of damaged cells before they can become malignant. However, in more than 50% of all tumors, mutations in p53 undermine its protective role, converting it into a driver of cancer.
In this study, the research team demonstrated that mutant p53 not only loses its tumor-suppressing abilities but also gains the capacity to corrupt other anti-tumor proteins, including p63 and p73. Through a mechanism known as aberrant phase transition, mutant p53 induces amyloid aggregation in p63 and p73, forming harmful protein clumps known as amyloid structures. These aggregates drive the oncogenic transformation of these proteins, leading to uncontrolled tumor growth.
The study also suggests that other proteins could be similarly affected, though further research is needed to identify them. These findings prov.