Investigating the Order of Recruitment of Mitochondrial Dynamic Proteins

Undergraduate Honors Thesis

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Citeable URL: https://scholar.colorado.edu/concern/undergraduate_honors_theses/zw12z695r

Abstract

Mitochondria are an essential organelle that produces most of the cell’s ATP and regulates apoptosis. Their morphology is integral to their function, and they undergo important dynamic events to maintain a healthy structure. Previous studies have shown that nodes on the endoplasmic reticulum (ER) regulate these dynamic fission and fusion events. Further, it has been shown that proteins associated with both events colocalize on the same sites. The actual mechanism of this colocalization is still largely unknown. The goal of this study was to characterize this colocalization and investigate the nature of their interactions. Through depleting cells of a fission protein (Drp1), we observed that a fusion protein (Mfn1) localization was also altered. This information provides groundwork on the nature of these proteins and how they interact. Future research into this interaction could provide insight into neurodegenerative diseases caused by inhibited mitochondrial dynamics.

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