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SETD2 Maintains Nuclear Integrity Through Mitotic Lamin Phosphorylation (2024)

Undergraduate: Phu Nguyen


Faculty Advisor: Abid Khan
Department: Biochemistry & Biophysics


The modification of histone tails is responsible for vital cellular processes such as DNA repair, chromatin organization, and transcription regulation. However, mutations in modifier enzymes, such as SETD2, are known to be linked to cancer and tumorigenesis. Although SETD2’s catalytic function of trimethylating H3K36 has been widely researched, we are focusing on its novel non-catalytic function with nuclear lamina, which is shown to be necessary for maintaining nuclear morphology and genome stability. The project provides evidence to the interaction between SETD2 and nuclear lamina by depleting SETD2 in synchronized cells and observing nuclear morphology post-mitosis. The results strengthen the causality of SETD2’s novel non-catalytic role during mitosis and its effect on nuclear morphology in the subsequent interphase.