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Generation Of Mutant Snap-23 To Arrest Mast Cell Degranulation At Trans-Snare Complex Formation, Suzette Wafford-Turner
Generation Of Mutant Snap-23 To Arrest Mast Cell Degranulation At Trans-Snare Complex Formation, Suzette Wafford-Turner
Honors Theses
Regulated secretion of pro-inflammatory molecules (e.g, histamines, proteases) from mast cells plays critical roles in immunity, allergic reactions, cardiovascular disease and cancer. These molecules are stored in secretory granules inside the cell and are rapidly released into the extracellular environment when mast cells are activated. It is known that mast cell degranulation depends upon membrane anchored SNAREs (soluble N-ethylmaleidimide-sensitive factor attachment protein receptors) and accessory proteins that form the trans-SNARE complex, a 4 helical bundle central to exocytic fusion. There are three SNARE proteins that contribute to the 4-helical bundle during exocytosis; Syntaxin and VAMP proteins each provide one helix …
Examining Interactions Between Opsins And Carotenoid Biosynthetic Proteins In Halophilic Archaea, Alexandru M. Plesa
Examining Interactions Between Opsins And Carotenoid Biosynthetic Proteins In Halophilic Archaea, Alexandru M. Plesa
Honors Theses
Organisms have evolved numerous specialized molecules for constantly responding to environmental changes. Examples of such molecules are the light-driven proton-pump rhodopsins, such as bacteriorhodopsin (BR) and cruxrhodopsin (cR), and the carotenoid pigments, such as retinal and bacterioruberin. In halophilic Archaea, retinal can covalently bind bacterioopsin (BO) and cruxopsin (CO) to form the corresponding protein complexes, and its biosynthesis is indirectly controlled by the activity of the lycopene elongase (Lye) enzyme, which converts lycopene, a retinal precursor, to a form of bacterioruberin. Interestingly, opsins were shown to inhibit the activity of Lye, thereby promoting retinal biosynthesis and indirectly regulating the apoprotein-cofactor …
Vesicle-Membrane Tethering: The Interaction Of Sec1 And Exocyst Subunit Sec6, Lauren O'Connor
Vesicle-Membrane Tethering: The Interaction Of Sec1 And Exocyst Subunit Sec6, Lauren O'Connor
Honors Theses
The exocyst complex is a multi-subunit tethering complex that is used in the process of exocytosis. There are eight subunits in the complex, and these subunits interact with each other as well as proteins outside of the complex to facilitate membrane fusion. Prior research has shown that the exocyst subunit Sec6 and Sec1 from the Sec1/Munc18 (SM) family, a known regulator of membrane fusion, interact with each other. In this experiment, the goal was to crosslink the two proteins and in turn work to identify the interacting amino acid residues that are responsible for the proteins’ interaction. To do this, …