Date of Graduation
Summer 2016
Degree
Master of Science in Biology
Department
Biology
Committee Chair
Kyoungtae Kim
Abstract
Yeast dynamin, Vps1, is a dynamic protein implicated in multiple trafficking pathways and at several cellular locations including the Golgi, endosome, and vacuole. Previous studies have found that Vps1 genetically and physically interacts with several ESCRT-II (Vps22, Vps36) and ESCRT-III (Vps2, Vps24) components. In light of these findings, little is known about how Vps1 functions with the ESCRT system. In my study, I have mapped the interaction domains between Vps1 and Vps22/Vps36 as well as explored the potential roles of these proteins during the targeting of vacuolar hydrolase, Cps1. My results support the idea of Vps1 working at the endosomal membrane and interacting with ESCRT-II towards the N-terminal end of its Vps22/Vp36 lobe. Additionally, a yeast two-hybrid library screen was performed in search of Vps1 binding partners. Here, I present seventeen novel binding partners. Based on these results, I have proposed a potential role for Vps1 in regulating chitin synthases during yeast cellular budding.
Keywords
Vps1, ESCRT, Protein Sorting, MVB, Yeast-Two Hybrid Screen
Subject Categories
Biology
Copyright
© Bryan Thien Banh
Recommended Citation
Banh, Bryan Thien, "Yeast Dynamin Functions With ESCRT-II At The Late Endosome And Potential Roles With Novel Binding Partners" (2016). MSU Graduate Theses/Dissertations. 2949.
https://bearworks.missouristate.edu/theses/2949
