How a Certain Protein Can Cause Deadly Cancers



It may be possible to develop more potent treatments for some of the most lethal types of cancer as a result of a discovery made by researchers at the University of California, Irvine on how a certain protein is activated in tumor cells. The discovery, which was spearheaded by researchers at the School of Biological Sciences, may one day lead to new therapeutic choices for skin cancer in adults and children, the most prevalent form of juvenile brain cancer, and the particularly hazardous melanoma and pancreatic adenocarcinoma. The study was released in the Life Science Alliance journal.

The discovery concerned the GLI1 protein, which is crucial for cell formation but has also been connected to a number of malignancies. GLI1 is often activated by the Hedgehog signaling pathway (HH), also known as HH. However, researchers have been aware for about ten years that the mitogen-activated protein kinase pathway and HH interact, or crosstalk, in ways that contribute to cancer.

A. Jane Bardwell, the study's lead author and a project scientist in the Department of Developmental and Cell Biology at UCI, explained that "under some circumstances, proteins in one route can turn on proteins in another." It's an intricate mechanism. We sought to comprehend the mechanistic mechanism by which proteins in the MAPK pathway activate GLI1.

In general, GLI1 and a protein called SUFU form a solid bind. GLI1 is inhibited by this protein, which stops it from entering cell nuclei and activating genes. The GLI1 protein may be phosphorylated or have a phosphate group added at seven different sites, which the researchers looked at.

According to Lee Bardwell, a professor of developmental and cell biology whose group carried out the experiment, "We identified three that can be phosphorylated and are important in decreasing the interaction between GLI1 and SUFU." As a result of this mechanism, GLI1 becomes activated and is able to reach cell nuclei, where it may induce uncontrolled cell growth and eventually cancer.

He observed that phosphorylation of all three sites results in much more GLI1 escape from SUFU than phosphorylation of just one or even two of the sites.

The discovery represents a substantial advance toward more precise and effective cancer therapies. It might be conceivable to produce a medicine tailored to a single tumor or individual patient if we can pinpoint exactly what is happening in a given disease or tumor, according to Bardwell. It would enable the treatment of these illnesses without the side effects of conventional chemotherapy. Additionally, different mutations exist in various tumors from the same malignancy in different people. In the future, it might be possible to screen tumors and determine the best course of action for each.

The National Cancer Institute, the National Institute of General Medical Sciences, the UC Cancer Research Coordinating Committee, and the Damon Runyon Cancer Research Foundation all provided funding for the study.

By UNIVERSITY OF CALIFORNIA, IRVINE

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