Identifying Novel Interactions Between Human Ubiquitin-Specific Protease 7 (USP7) and Histone Methylating/Demethylating Proteins

The deubiquitinase, Ubiquitin-Specific Protease 7 (USP7) is an indispensable protein responsible for regulating appropriate turnover of proteins involved in numerous signaling pathways and biological processes including immune response, DNA damage response, DNA replication, epigenetics and cell division. USP7s role in epigenetics is emerging and studies have demonstrated that USP7 modulates several epigenetic modifiers. This thesis further explores USP7s role in epigenetics, investigating USP7s novel regulation of two histone modifying enzymes highly implicated in oncogenesis, Enhancer of Zeste Homolog 2 (EZH2) and Retinoblastoma Binding Protein 2 (RBP2). Based on previous findings, our group identified probable interaction sites in these proteins and pursued to characterize the interactions and regulatory relationships.