Protein aggregation ― the localized accumulation of misfolded proteins ― is believed to contribute to human diseases from neurodegeneration to diabetes. Work published this week in Nature Chemical Biology suggests that cancer unexpectedly may share this underlying pathology.
Proteins often adopt specific three-dimensional structures that are necessary for them to fulfill their cellular function. The tumor suppressor p53, which is mutated in nearly half of all cancers, is no exception. Now Frederic Rousseau, Joost Schymkowitz and colleagues have identified a segment of p53 that is exposed in mutated versions of p53 that are structurally destabilized. This segment can seed protein aggregation and interfere with the function of not only normal p53 but of other related proteins as well. These new data provide insight into how some mutations in p53 can disrupt the activity of other proteins and thereby promote tumor progression.
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