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

File Format

PDF

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