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Ubiquitylation and Phosphorylation Regulate Cell Cycle Progression

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Cell division and cell cycle progression are regulated by various proteins. The activity of these proteins are fine-tuned by post-translational modifications such as ubiquitylation and phosphorylation. Identifying what proteins are modified, the enzymes that performed the modification, and the consequence of the modification has been a core component of understanding the regulation of cell cycle progression. Here, I present my thesis on examining various aspects of these post-translational modifications as they apply to cell cycle progression. First, I discuss the Cul3 substrate adaptor SPOP and its role in regulation of Nup153. Next, I discuss KCTD proteins and their ability to bind to Cul3. Finally, I characterize Cdk15, a putative spindle assembly checkpoint kinase. Altogether, these projects further our understanding of how enzymes and their post-translational modifications orchestrate the various processes necessary for cell division and cell cycle progression and how misregulation of these processes may lead to certain disease states like cancer.

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This item is under embargo until June 10, 2024.