Author

Grace Dittmar

Date of Award

5-2019

Degree Type

Honors College Thesis

Department

Biological Sciences

First Advisor

Hao Xu, Ph.D

Advisor Department

Biological Sciences

Abstract

Exocytosis is the process by which cells release various molecules into the extracellular space. This mechanism is accomplished by membrane fusion, in which the membrane of the transport vesicle and that of the cell itself fuse to create one continuous membrane, allowing the release of the molecules inside the vesicle. A family of proteins, known as SNARE proteins, is responsible for facilitating membrane fusion. SNARE proteins form a complex between the vesicle membrane and the plasma membrane. For various cells, such as mast cells and neurons, exocytosis is essential to carry out their vital functions. Various accessory proteins are known to play a role in membrane fusion by regulating the assembly and disassembly of the SNARE complex. One family of proteins is known as Munc13 proteins. This protein family has been shown to regulate SNARE complex formation both positively and negatively in mast cells and neurons. While three isoforms are cell-specific, Munc13-1 has been found to regulate degranulation in both neurons and mast cells. In mast cells, Munc13-1 has been found to inhibit the activity of degranulation stimulating protein Munc13-4, and to decrease the level of antigen-induced degranulation experienced by the cell. However, in neurons, Munc13-1 helps to convert syntaxin from the closed Munc18-syntaxin formation to the open SNARE complex formation. This project aims to transform two expression systems with a truncated version of Munc13-1 gene from two different plasmids to use in further studies.

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