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Phosphorylation of Orb2 by Wnd
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Wallenda (Wnd) is an evolutionarily conserved protein kinase that is essential for neural development including axon branch development, axon regeneration and degeneration. However, the molecular mechanisms underlying Wnd action is not fully understood. Kim lab recently has found Orb2 as a novel Wnd pathway. Orb2 is one of the cytoplasmic polyadenylation factors that control the length of poly (A) tail in its target mRNAs. This suggests that Wnd controls neural development through Orb2 phosphorylating. To study the biological function of Orb2 phosphorylation by Wnd, it is essential to map the phosphorylated amino acid residues in Orb2 by Wnd kinase. We have mapped the phosphorylated Serine and Threonine residues in Orb2 upon Wnd co-expression in cultured Drosophila S2 cells using phospho-proteomics. Subsequently, we generated the mutant Orb2 that are defective in Wnd-mediated phosphorylation as well as the mutant Orb2 that mimics the phosphorylated version of Orb2. Wnd regulates the expression of Dscam. The expression regulation of Dscam by Orb2, and the effect of Orb2 phosphorylation by Wnd in this process will be discussed.