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Abstract
The canonical function of RGS10 (regulator of G-protein signaling) is to terminate G-protein activity by accelerating GTPase activity on the G subunit. Previous research has shown that under inflammatory conditions, RGS10 can suppress inflammatory cytokines. However, this function of RGS10 is G-protein independent. To investigate whether inflammation changes the subcellular localization of RGS10, a palmitoylation deficient RGS10 mutant (RGS10 C74A) was created. Palmitoylation is a post translational modification that enhances RGS10 association with the cell membrane. It was found that under inflammatory conditions, both wild-type RGS10 and RGS10 C74A exhibited higher protein expression than empty vector control at the membranes and nucleoplasm. Furthermore, there was no significant difference between wild-type RGS10 and RGS10 C74A in suppressing the inflammatory cytokine TNF. It was concluded that palmitoylation is not required for RGS10s subcellular localization or function in suppressing inflammation. Further investigation is needed to understand the role of RGS10 in the nucleoplasm.