High-throughput screening for kinases and phosphatases regulators.
- Identifies regulators of kinases and phosphatases by their interaction with 14-3-3 proteins.
- Eliminates the need for radiolabeled tracers or antibodies when screening.
- Ideal method for high-throughput screening.
Phosphorylation is a common post-translational modification used to regulate many cellular processes. Phosphate groups are added to targets (usually a protein or peptide) by kinase enzymes and removed via phosphatase enzymes. The addition or removal of phosphate groups changes the function of a target by altering its enzyme activity, its cellular location, or its interaction with other proteins. Specific kinases and phosphatases modulate specific targets that are often involved in disease states. Thus, identifying kinases and phosphatases quickly and efficiently offers a way to identify new therapeutic targets for drug discovery.
This invention provides a novel high-throughput screening method for kinase and phosphatase regulators by exploiting their phosphorylation-dependent interactions with 14-3-3 proteins. 14-3-3 proteins have the ability to bind many signaling proteins, and their binding is key to regulating the cell cycle, especially in the central nervous system. Additionally, disregulation of 14-3-3 regulation has been implicated in various types of cancer. Current screening methods involve either the use of radiolabeled tracers or site specific antibodies, the generation of which can be both costly and time consuming. This invention eliminates these limitations, providing a single system which can be used for quick and efficient screening.
Developmental Stage & Potential Market
- This screening method has been used by the inventor for laboratory research.
- The kinase-targeted drug market is expected to reach approximately $58 billion by 2010.