Degree Type
Creative Component
Semester of Graduation
Spring 2020
Department
Biomedical Sciences
First Major Professor
Jinoh Kim
Degree(s)
Master of Science (MS)
Major(s)
Biomedical Sciences
Abstract
Protein secretion is essential for cell viability. A large variety of secretory and membrane proteins are secreted through the secretory pathway. Studies have revealed how these proteins are secreted by analyzing the components of the secretory pathway. The coat protein complex II (COPII)-coated vesicles are responsible for generating vesicles at the endoplasmic reticulum. During the COPII vesicle assembly the COPII proteins package cargo molecules to nascent vesicles. COPII vesicles then fuse with ER/Golgi intermediate compartment in mammalian cells or the Golgi apparatus in yeast. The COPII proteins consist of Sar1, Sec23/Sec24 complex, and Sec13/Sec31 complex. There are paralogs of most of these proteins in vertebrates which partly explain how COPII vesicles package a large variety of proteins. Mutations in one paralog can have devastating effects on the individual, while mutations in another paralog may only cause mild health issues. By understanding how these COPII proteins function and which proteins they interact with, we can learn more about diseases caused by mutations in the genes and possibly find ways to cure or better manage these diseases.
Copyright Owner
Concannon, Cassandra
Copyright Year
2020
File Format
Recommended Citation
Concannon, Cassandra, "Mutations in the COPII Vesicle Genes and the Diseases they Lead to" (2020). Creative Components. 484.
https://lib.dr.iastate.edu/creativecomponents/484