Emory biochemist writes lead essay describing Nobel Prize research on ubiquitin protein

12/15/04

Dr. Keith Wilkinson was laboratory associate during discoveries leading to 2004 Nobel Prize in Chemistry

ATLANTA During the late 1970s Emory University School of Medicine biochemist Keith D. Wilkinson, PhD, was a research fellow in the laboratory of Dr. Irwin Rose at the Fox Chase Cancer Center in Philadelphia. Dr. Wilkinson was part of the team that discovered the key biological function of the ubiquitin protein, which helps regulate cells by "tagging" cellular proteins that need to be eliminated when they become defective or are no longer necessary for a particular cell. Last week Dr. Rose, now at the University of California, Irvine, was one of three scientists awarded the Nobel Prize in Chemistry for the discovery of "ubiquitin-mediated protein degradation." The other two scientists were Avram Hershko and Aaron Ciechanover of the Israel Institute of Technology. Dr. Wilkinson was invited as an honorary guest to the Nobel ceremonies in Stockholm, Sweden on December 10.

Today, says Dr. Wilkinson, it is almost impossible to conduct research in any area of the biological sciences without recognizing the impact of the ubiquitin system. His Nobel essay, entitled "Ubiquitin: A Nobel Protein," appears in the December 17 issue of the journal Cell. His laboratory still conducts highly regarded research on the proteolysis system, which regulates the amounts and the location of proteins in cells with the help of ubiquitin. Dr. Wilkinson is a professor of biochemistry in Emory School of Medicine and director of Emory University's Graduate Division of Biological and Biomedical Sciences.

"The research on the ubiquitin pathway, including Dr. Wilkinson's work, is important because it provides more detailed information about cell survival and death," says Bryan Noe, PhD, professor of cell biology in Emory University School of Medicine and acting director of Emory's Graduate School of Arts and Sciences. "All cells have a prescribed lifespan, some very short, and some very long. The rates of protein turnover are important in determining how long a cell can survive, and the ubiquitin system helps regulate those rates. In certain disease states, protein breakdown rates can accelerate to a rate greater than normal, thus altering the cells' ability to repair themselves, and ultimately leading to premature cell death."

Dr. Wilkinson's essay in Cell traces the history of the groundbreaking research on ubiquitin over the past 25 years. It is remarkable, he notes, that it took so long to discover a system that plays such a central role in a variety of pathways in the cell and also notable that the entire system has now been so well defined.

"These discoveries present us with enormous opportunities to develop drugs that could target various aspects of the ubiquitin pathway," Dr. Wilkinson says. "Because we now have so much detailed information about ubiquitination, these new drugs could be highly selective. Ubiquitin is an example of the way in which scientific research that begins by focusing on a narrow question can lead to a vast amount of knowledge about a key biological system."

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