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Study reveals molecular key to tumor suppressor activity

so determined that phosphorylation occurs in that area," Xiong said. "We discovered this in normal cells, but we can also take tumor cells in which p53 is not working and insert functioning p53 into the nucleus and it will remain there."

In addition to further understanding a cellular control mechanism of p53, Xiong's findings have other implications.

"Protein transport is a major regulator of cellular function. This represents one of the first examples where a nuclear exporting signal can be regulated by phosphorylation," he said.

"In half of all tumor cells p53 is not working, sometimes because a kinase gene responsible for p53 phosphorylation is mutated. When that gene is broken, DNA damage cannot be repaired because P53 is continually exported to the cytoplasm and getting degraded there. So one could imagine if we were to develop a compound to block p53 export, we might be able to restore p53 function in tumor cells with mutated kinase genes. We could give the compound to patients to wake up the p53 or prevent its degradation."

Thus the new study explains the molecular site of an all-important effect on p53 of phosphorylation. "By continuing this line of research we hope to understand exactly how the phosphate signal shuts the door on p53 export," Xiong said. "That knowledge can be used to develop a targeted treatment for malignant tumors."


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Contact: Leslie Lang
llang@med.unc.edu
919-843-9687
University of North Carolina School of Medicine
7-Jun-2001


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