Investigating the Role of 14-3-3[zeta] SUMOylation
Author | : Hoang Anh Phuc Nguyen |
Publisher | : |
Total Pages | : 39 |
Release | : 2013 |
Genre | : |
ISBN | : |
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SUMO modification is involved in several cellular processes such as signal transduction, cell division, and regulation of protein subcellular localization, specifically including Ras signaling and protein nuclear import/export. Previous studies have demonstrated that 14-3-3[zeta], which is thought to have functions in both the nucleus and cytoplasm, is a SUMOylated protein and is required for Ras signaling. I have therefore sought to determine whether or not the SUMOylation of 14-3-3[zeta] promotes or inhibits its localization to the nucleus. Subcellular fractionation experiments fail to reveal a detectable change in the overall ratio of nuclear to cytoplasmic 14-3-3[zeta] upon knockdown of SUMO by RNAi in cultured Drosophila cells. However, immunofluorescence studies suggest that nuclear localization of this protein may increase in a subset of the SUMO knockdown cells.