Phosphorylation is a cellular process that modifies proteins, and thereby regulates the cellular fates of more than two-thirds of all proteins. This dynamic process is carried out by protein kinases, which phosphorylate specific proteins to regulate a variety of downstream cellular mechanisms, including development and functioning of the nervous system. SRPK is one such protein kinase that phosphorylates proteins to control gene expression, the cell cycle, and cell survival in neurons. Previous work from the lab has demonstrated that SRPK phosphorylates RNF12/RLIM, a member of the E3 ligase family of enzymes that control protein destruction. SRPK phosphorylation of RNF12 controls destruction of proteins involved in gene expression, to regulate expression of neuronal genes. Patient mutations in the gene encoding RNF12 cause Tonne-Kalscheuer syndrome (TOKAS), an intellectual disability disorder. SRPK also phosphorylates other E3 ligases that have important functions in the nervous system. These include RNF10, which is linked to control of protein translation, formation of neurons, and protecting neurons with a myelin sheath. In this project, I aim to understand how SRPK phosphorylation controls RNF10 and to understand the downstream consequences for development and functioning of neurons in the nervous system.