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Name of Student: Dominik Sommerfeld Research Supervisor: Dr. Catherine Pallen Title of Presentation: The role of specific Protein Phosphatase 2A (PP2A) holoenzymes in orchestrating the cell cycle symphony Abstract Protein phosphatase 2A (PP2A), a highly abundant, ubiquitous and conserved Ser/Thr-specific phosphatase, has been shown to regulate a plethora of important cellular processes, including the cell cycle progression. PP2A is a heterotrimeric holoenzyme complex composed of a catalytic subunit, a scaffolding subunit, and a variable, regulatory subunit. Genetic alterations in the scaffolding subunit and genomic deletions or loss of heterozygosity (LOH) of regulatory subunits have been identified in various cancers, including breast, ovarian and cervical carcinomas. In particular, recurrent genomic deletions of the PPP2R2A (B55alpha) and PPP2R3B (PR70/48) subunits have been found in specific subtypes of luminal breast and endometrial carcinoma. Therefore, it is likely that dysregulation or dysfunction of PP2A holoenzymes containing these specific subunits plays an important role in these cancers. Many potential downstream targets of PP2A dysregulation have been reported, including cell cycle regulators. Specifically, the B55alpha regulatory subunit has been implicated in the regulation of mitotic entry and exit, while the PR70/48 subunit is believed to be involved in regulation of DNA replication. Our aim is to investigate the functional consequences of loss of the B55alpha and PR70/48 subunits on cell cycle control, and to elucidate underlying molecular pathways, so as to gain insight into the roles of PP2A genetic alterations in cancer.