Abstract

Mulan is an E3 ubiquitin ligase and an E3 SUMO ligase embedded in the outer mitochondrial membrane. Mulan plays a major role in various cell processes including cell growth, mitophagy, apoptosis, and mitochondrial dynamics. In addition, its deregulation is involved in the development and progression of several human disorders such as neurodegeneration and heart disease. There are two main discernible domains in Mulan: a large cytoplasmic domain that encodes the RING-finger motif and carries out the catalytic activity of the protein; the second domain of Mulan is exposed to the intermembrane space of mitochondria, and its function remains unknown. This part of Mulan is also referred to as the BAM domain and is expected to have a significant function since its amino acid sequence has been conserved through evolution and is found in bacteria, animals, and plants. The purpose of this study is to isolate and characterize potential binding partner proteins of the BAM domain using the yeast two-hybrid system. These studies are expected to provide new information on the physiological function of this domain and how it is potentially used to modulate the ligase activity of Mulan.

Thesis Completion

2016

Semester

Fall

Thesis Chair/Advisor

Zervos, Antonis S.

Degree

Bachelor of Science (B.S.)

College

College of Medicine

Department

Burnett School of Biomedical Sciences

Degree Program

Biomedical Sciences

Location

Orlando (Main) Campus

Language

English

Access Status

Open Access

Length of Campus-only Access

5 years

Release Date

6-1-2022

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