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- W2073409849 abstract "The SNARE protein SNAP-25 plays a critical role in neuronal exocytosis. The linker region of SNAP-25 contains 4 cysteines (cysteine-rich domain) which are the sites of various post-translational modifications, such as palmitoylation and oxidation. Palmitoylation anchors SNAP-25 to the membrane (and determines its distribution within the cell), while the level of oxidation may regulate neurotransmitter release.Quantifying the extent of oxidation and palmitoylation in vivo has proven elusive. Our in vitro data from SNAP-25 suggests that non-enzymatic palmitoylation is cooperative with a Hill Coefficient greater than 2, whereas oxidation appears to have a Hill coefficient of 1/2 (consistent with two cysteines being consumed for each oxidation event). Using Circular Dichroism to measure the melting of helical structures of SNAP-25, we show that oxidation destabilizes SNAP-25. Oxidation also destabilizes SNARE complex formation. During in vitro palmitoylation, we use Mass Spec analysis to confirm that multiple cysteines are palmitoylated under our conditions. In vitro palmitoylation and oxidation have an EC50 of about 50 μM. Through additional experimentation we hope to elucidate the EC50, Hill Coefficient, and extent of reaction for enzyme-catalyzed palmitoylation of the cysteine-rich domain of SNAP-25's linker region and also determine how oxidation and palmitoylation alter SNARE complex formation." @default.
- W2073409849 created "2016-06-24" @default.
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- W2073409849 date "2014-01-01" @default.
- W2073409849 modified "2023-09-30" @default.
- W2073409849 title "In Vitro Palmitoylation and Oxidation of the Snare Protein SNAP-25" @default.
- W2073409849 doi "https://doi.org/10.1016/j.bpj.2013.11.1801" @default.
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