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Drosophila melanogaster Protein Kinase CK2 Interacts with and Phosphorylates the Neurogenic Repressor m8 Resulting in the Production of a Novel Eye Phenotype Regina L. Trott Protein kinase CK2 is a serine/threonine protein kinase ubiquitously expressed in eukaryotic organisms. The enzyme is composed of 2 α (catalytic) subunits and 2 β (regulatory) subunits. The minimum consensus site for CK2 phosphorylation is S/TXXD/E, where “X” is any non-basic amino acid. Substrates so far identified include proteins associated with cell cycle regulation and development. In Drosophila melanogaster, the Notch pathway activates members of the Enhancer-of-split Complex [E(spl)-C]. m8, which is a member of the E(spl)-C, was found to interact with and be phosphorylated by CK2. The physiological affects of CK2 phosphorylation were studied in vivo through the Gal4-UAS system. Flies with a reduced eye phenotype were identified in a cross between scaGal4 and the transgenic line m8SD. Two-hybrid analysis indicated m8SD interacted significantly stronger with the proneural bHLH protein Atonal than either m8 or m8SA. These results are the first indication that phosphorylation plays a role in the regulation of E(spl)-C proteins and also the first implication of a role for CK2 during neurogenesis.

Drosophila melanogaster protein kinase CK2 interacts with and phosphorylates the neurogenic repressor m8 resulting in the production of a novel eye phenotype