Novel Functions of EZH2 in Triple-Negative Breast Cancer: Translation into New Biomarker and Treatment Strategies
Technical Report,01 Jul 2015,30 Jun 2016
Regents of the University of Michigan Ann Arbor United States
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In the first year of funding we have been able to characterize the protein-protein interactions PPIs betweenEZH2 and p38 and with AKT1. We successfully determined the kinetic and binding affinity of these PPIs usingrecombinant full length proteins. These results confirmed the direct interactions between EZH2 and p38 andAKT1 as well as the co-immunoprecipitations studies which showed that EZH2 binds to p38in both the nucleusand the cytoplasm of MDA-MB-231 cells. We will continue with biochemical and biophysical studies towardsmapping the binding site and identifying the key residues essential for these PPIs.