Date of Award
4-27-2021
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Mathematics and Statistics
First Advisor
Hassan Elsalloukh
Abstract
The Golgi is the central organelle of the protein transportation in eukaryotic cells. Vesicle tethering and fusion on Golgi needs a special tether molecule called Conserved Oligomeric Golgi Complex (COG). Since COG is not naturally a membrane protein, how COG remains on the Golgi during vesicle tethering and fusion is unclear. In this project, direct COG binding to three types of Golgi molecules were tested. Golgi SNAREs STX5, GS28, and GS15 are capable of binding to COG to a different extent, while Golgi SNARE Ykt6 has a poor binding to COG. Lysosomal SNARE STX7 has very low level of COG binding, indicating COG prefers to interact with Golgi SNAREs. Golgi Rabs Rab2a and Rab30 can bind to COG similarly. Also, Golgi lipid PI4P can interact with COG. These results indicate that Golgi SNAREs, Rabs, and lipids all contribute to the association of COG to the Golgi.
Recommended Citation
Wang, Wei, "In Vitro Study of COG Complex Association with Golgi Membrane" (2021). Theses and Dissertations. 1000.
https://research.ualr.edu/etd/1000
