Key to common cancer pathway

ScienceDaily | 3/18/2019 | Staff
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These dueling qualities make the p53 protein and the gene that makes it among the most studied in biology, yet the molecular mechanisms that govern its stability and function have yet to be fully understood.

Writing this week (March 18, 2019) in the journal Nature Cell Biology, a team led by University of Wisconsin-Madison cancer researchers Richard A. Anderson and Vincent Cryns reports the discovery of an unexpected regulator of the critical protein, opening the door to the development of drugs that could target it.

P53 - Janus - Anderson - Roman - God

"p53, like Janus, has two faces," says Anderson, referencing the Roman god of gates and doorways. "The p53 gene is the most frequently mutated gene in cancers, and when mutated it switches its function from a tumor suppressor to an oncogene that drives the majority of cancers."

Typically, explains Anderson of the UW School of Medicine and Public Health, the p53 protein serves as "the guardian of the genome," initiating the repair of DNA damaged by ultraviolet radiation, chemicals or other means and preventing tumor growth. When mutated, however, the protein goes rogue, becoming more stable and abundant than its unmutated counterpart, accumulating in the nucleus of the cell and causing cancer.

Research - Team - Study - Authors - Fellows

The research team, which includes study lead authors and postdoctoral fellows Suyong Choi and Mo Chen, found a new mechanism that drives this stability. The culprit: an enzyme called PIPK1-alpha and its lipid messenger, known as PIP2, which seem to behave as master regulators of p53.

The Wisconsin team showed that when a cell is stressed, whether by DNA damage or other means, the enzyme associates with...
(Excerpt) Read more at: ScienceDaily
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