Date of Award
Doctor of Philosophy
Biochemistry, Biophysics and Molecular Biology
Yeon-Kyun . Shin
For decades α-synuclein has been the focus of research because of its association with Parkinson's disease and other types of dementia. Recently the focus has shifted from attempting to understand the mode of toxicity of α-synuclein aggregates to trying to identify α-synuclein's healthy physiological function. It has been identified that α-synuclein interacts with the SNARE complex and assists in SNARE-mediated membrane fusion. Utilizing two novel single molecule assays we are able to determine how α-synuclein enhances SNARE
activity. α-synuclein has two major domains: one that buries itself in the phospholipid head groups of a membrane and another that binds to the v-SNARE VAMP2. By using both of these domains α-synuclein can tether vesicles more securely to the plasma membrane providing the SNARE complex more time to form properly.
Brenden James Douglas Hawk
Hawk, Brenden James Douglas, "Insights into the native function of α-synuclein" (2019). Graduate Theses and Dissertations. 17693.