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Study shows how mutant protein clusters drive disease-causing aggregates A mutation that replaces a single amino acid in a potent tumor-suppressing protein turns it from saint to sinister. A new study by a coalition of Texas institutions shows why that is more damaging than previously known. The ubiquitous p53 protein in its natural state, sometimes called “the guardian of the genome,” is a front-line protector against cancer. But the mutant form appears in 50% or more of human cancers and actively blocks cancer suppressors. Researchers led by Peter Vekilov at the University of Houston (UH) and Anatoly Kolomeisky at Rice University have discovered the same mutant protein can aggregate into clusters. These in turn nucleate the formation of amyloid fibrils, a prime suspect in cancers as well as neurological diseases like Alzheimer’s.

University of houstonUnited statesRice universityUniversity of texasDavid yangNavin varadarajanAram davtyanMichelle bartonMohsen fathiArash saeediAlena klindziukPeter vekilovMichael shermanKolomeisky research group rice universityRice department of chemistryNational science foundation