The protein, known as raf kinase inhibitor protein (RKIP) controls activity of kinases, a type of enzyme that acts as a key component in the biochemical signaling pathways responsible for determining almost all cellular activity. But RKIP’s own activity is inhibited when a small molecule organic compound called locostatin binds to it.
The researchers from the University of Illinois at Chicago (UIC) used an approach sometimes called “forward chemical genetics” whereby they first identified locostatin as an inhibitor of cell migration, then used locostatin itself as a kind of bait to fish out the protein to which it binds. That protein was RKIP.
As a regulatory protein, RKIP controls the functions of kinases, thereby governing signaling pathways. When these pathways are not properly controlled, all kinds of diseases can result, including cancer.
“The interest in RKIP now is that it is a new and apparently important modulator of cell migration and therefore a possible target in anticancer strategies focused on limiting tumor angiogenesis and metastasis,” said Dr Gabriel Fenteany assistant professor of chemistry at UIC and lead investigator.
More investigation on how exactly RKIP controls cell migration is needed, Fenteany said. UIC researchers are also trying to determine the potential of locostatin as a drug by looking at its effects on different types of cells and tissues.