CHAPEL HILL, NC Cancer occurs when human cells move and multiply inappropriately. Within cells, a process called phosphorylation serves as an on/off switch for a number of cellular processes that can be involved in cancer, including metabolism, transcription, configuration, movement, cell death and differentiation. This process is controlled by a group of enzymes called protein kinases that working together and separately modify the structure of proteins, changing them and allowing them to control cellular processes.
One of the challenges to understanding the actions and interactions of kinases within cells has been that the mechanisms scientists used to control the enzymes were not specific, often affecting more than one pathway within the cell.
In a paper published today in the journal Nature Biotechnology, Klaus Hahn, PhD, who is the Thurman Professor of Pharmacology at the University of North Carolina at Chapel Hill and a member of UNC Lineberger Comprehensive Cancer Center, describes a new technique called engineered allosteric regulation, which provides a new tool for scientists who study the interactions of proteins within living cells.
"Engineered allosteric regulation is a new method that provides precise control of kinase activity in living cells," said Hahn.
"We can now take the kinase of choice and precisely control the 'on/off' switch, thereby seeing what they are doing and how they control cell function. The technology has exciting applications in basic research, since kinases are the central regulators of almost every cellular process. The ability to precisely control the state and timing of kinase action within cells opens the door to a broad range of new scientific insights," he added.
"This ingenious method offers a powerful new approach for dissecting the diverse functions of kinases in living cells," said James Deatherage, PhD, who oversees cell biology grants at the NIH's National Institute of Gene
|Contact: Ellen de Graffenreid|
University of North Carolina School of Medicine