Nature's Supplement: From the tumor suppressor gene to the oncogene, this protein has "two faces" March 20, 2019 Source: Biological Exploration Scientists have long known about p53, a mutation that is a key factor in the pathogenesis of many different types of cancer. However, its unmutated form prevents cancer. These "two-sided" characteristics make p53 protein and regulatory genes one of the most biologically studied subjects. But the molecular mechanisms that regulate its stability and function are not fully understood. A team led by cancer researchers at the University of Wisconsin-Madison, Richard A. Anderson and Vincent Cryns, discovered an unexpected regulator of this key protein for the development of drugs for this protein. Opened the door. The findings were published in the journal Nature Cell Biology. Https://doi.org/10.1038/s41556-019-0297-2 The p53 protein is usually the "guardian of the genome", which initiates repair of DNA that is destroyed by ultraviolet light, chemicals or other means and prevents tumor growth. However, when a mutation occurs, the protein becomes out of control and becomes more stable and richer than the unmutated one, accumulating in the nucleus, leading to cancer. "P53, like the Roman door god Janus, has two faces," Anderson said. "The p53 gene is the most frequently mutated gene in cancer. When a mutation occurs, its function is from tumor suppression. Genes turn into oncogenes that drive most cancers." The team found a new mechanism to drive this stability – the culprit is an enzyme called PIPK1-alpha and its lipid messenger PIP2, which appears to be a major regulator of p53. Whether through DNA damage or other means, when the cells are stressed, the enzyme binds to p53, producing PIP2, which binds tightly to the cell and promotes the interaction between p53 and a molecule called a small heat shock protein. This stabilizes the protein complex and lays the foundation for the development of cancer, including malignant tumors such as triple-negative breast cancer. "Small heat shock proteins are really good at stabilizing proteins," Cryns said. "In our study, their combination with mutant p53 may promote their cancer-promoting effects, which we are actively exploring." In this new study, the researchers also found that when the PIP2 enzyme pathway is disrupted, the mutant p53 does not accumulate and cause damage. This also means that if you can eliminate the mutation of p53, you may be able to eliminate the cancer driven by p53. Currently, researchers are actively looking for inhibitors of the PIPK1-alpha enzyme that can be used to treat tumors with p53 mutations. Cryns pointed out that "although p53 is one of the most common mutations in cancer, we still don't have any drugs specifically for p53. Our findings on this new molecular complex suggest that there are several different ways to p53 As a target of destruction, including blocking kinases or other molecules that bind to p53." Greenhouse Vertical Hydroponics
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Nature's Supplement: From the tumor suppressor gene to the oncogene, this protein has "two faces"