Sanford-Burnham Medical Research Institute
posted on 07/07/2009
A method for assaying ubiquitination and identifying modulators of ubiquitination to regulate aberrant signal transduction.
Â· Multi-well array analysis for high throughput screening
Â· Can be used independent of the E3 ubiquitination enzyme
Ubiquitin is a highly conserved protein expressed in all eukaryotic cells. The levels of many intracellular proteins are regulated by a ubiquitin-dependent proteolytic process. This process involves the covalent ligation of ubiquitin to a target protein, resulting in a poly-ubiquitinated target protein that is rapidly detected and degraded. The ubiquitination of these proteins is mediated by a cascade of enzymatic activities, with E3 being the final enzyme used in the cascade. In this process, chains of ubiquitin are formed on the target protein, each covalently ligated to the next through the activity of E3. Modulators of ubiquitination can be used to upregulate or downregulate specific molecules involved in cellular signal transduction. Disease processes can be treated by such up- or down regulation of signal transducers. Due to the importance of ubiquitination in cellular regulation, the current invention provides a means for assaying ubiquitination and identifying modulators of ubiquitination.
John C. Reed, M.D., Ph.D.
Full title: E3- independent ubiquitinylation assay
U.S. Patent/Application #: 61/048,796
Priority date: 4-29-2008
Foreign filing: tbd
Burnham ID: 08-024
File Number: 08-024/REED*
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