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UC LEADS is more than an opportunity, it is a great gift. I have never felt so privileged or honored to be part of a program impacted with such exceptional standards in leadership, outstanding educational goals and a focus to develop strong mentor/scholar relationships. The UC LEADS program has taken the minute scope of information I had about graduate school and broadened it a hundred times. Dedicated to the success of their scholars, they have provided me with numerous and extensive experiences in becoming a more promising graduate applicant. Through UC LEADS I have been able to conduct cutting-edge research in my field of study, Cellular Biology. Additionally, to strengthen my résumé, I have had the opportunity to present this research at conferences all over the nation. The skills and tools I have gained and the relationships I have built over are invaluable and without them my education at UC Davis would not be as complete or rewarding.
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Dissecting the Role of Dnm1 in Mitochondrial Fission
Selena Martinez, Elena Ingerman and Jodi Nunnari
Molecular and Cellular Biology, University of California, Davis
Mitochondria are essential organelles that generate the cell's energy source-ATP. Organelle morphology influences mitochondrial function and is established and maintained by two opposing processes: fission and fusion. The focus of this project is on the mechanism of mitochondrial fission, which, in the model system Sacchaormcyes cerevisiae, is mediated by three proteins: Dnm1, Mdv1, and Fis1. Dnm1 is a dynamin-related GTPase that self assembles into spiral-like structures that target to and associate with mitochondria and likely promote membrane constriction and fission. The mechanism by which Dnm1 specifically associates with mitochondria and how Dnm1 promotes membrane constriction and fission is unknown. To address these questions, a detailed structure-function analysis of Dnm1 has been undertaken. Specifically, I will use site-directed mutagenesis to change conserved residues in Dnm1’s middle, insert B, and GTPase effector domains, that we have postulated function in membrane targeting and assembly. This approach will allow us to gain insight into the mechanism of mitochondrial fission.
Using the Yeast Two-Hybrid System to Examine and Elucidate the Unknown Mechanisms that Mediate Mitochondrial Fission
Selena Martinez, Elena Ingerman and Jodi Nunnari
Molecular and Cellular Biology, University of California, Davis
Mitochondria, which are essential organelles, generate most of a eukaryotic cell's adenosine triphosphate (ATP), a form of energy that is imperative for cell function. Additionally, mitochondria are required for amino acid synthesis. Mitochondrial structure, which influences the function of these essential organelles, is maintained by two opposing processes: fission and fusion. Many of the components of mitochondrial dynamics are evolutionarily conserved. The focus of this project is mitochondrial fission, which, in our model system, the yeast Saccharomyces cerevisiae , is mediated by three proteins: Dnm1, Mdv1, and Fis1. In order to better understand the mechanistic interplay among the fission components, we are using the yeast two-hybrid system in order to examine protein-protein interactions between Dnm1 and Mdv1.
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