Date of Graduation
Summer 2020
Degree
Master of Science in Biology
Department
Biology
Committee Chair
Kyoungtae Kim
Abstract
To maintain cell homeostasis, protein recycling through intracellular membrane fusion is an important cellular process. Both Vps1 and Ypt6 have been implicated in protein recycling from the endosome to the trans-Golgi Network (TGN). SNARE proteins are thought to be the key regulator in this membrane fusion mediated protein recycling mechanism. I studied membrane fusion events by incorporating purified proteins into liposomes. A series of data suggest that high concentration of SNARE proteins inhibits fusion unlike the opposite popular notion. Also, the data suggests that Vps1 acts on membrane fusion dynamics in a manner that lower concentrations of Vps1 enhance fusion in compared to its higher concentration counterpart. Moreover, it was found that Vps1’s GTPase activity seems to be inadequate to enhance fusion. Finally, the data suggests that Vps1 and Ypt6 do not act in a synergistic mode despite both of them possessing GTPase activity.
Keywords
membrane fusion, Vps1, Ypt6, SNARE, reconstitution assay, GTPase activity
Subject Categories
Biochemistry
Copyright
© Ehsan Suez
Recommended Citation
Suez, Ehsan, "Multifaceted Mechanism of Vps1 Mediated Endosome-to-Golgi Fusion in Vitro" (2020). MSU Graduate Theses. 3542.
https://bearworks.missouristate.edu/theses/3542
