JIL-1 has recently been characterized as a protein kinase implicated in dosage compensation and chromosomal organization. To further understand its role in Drosophila, plasmid constructs to be injected into transgenic flies have been created which carry truncated JIL-1 sequences ligated to that of fluorescent proteins. One fluorescent fusion construct that contains the carboxy-terminal domain of JIL-1 was microinjected into Drosophila by use of P element vectors and expressed with GAL4 driver lines. The protein can be visualized in numerous tissue, and localizes to polytene chromosomes from salivary glands. This will be used in future experiments to determine roles of the carboxy-terminal domain of JIL-1 by studying it's localization and phenotypic affects. Also, JIL-1's interactions with other proteins was investigated by testing its possible binding to lamin protein. JIL-1 was found to co-immunoprecipitate with lamin from S2 cells and Drosophila embryos. GST fused to the carboxy-terminal domain of JIL-1 was used in GST pull down assays to show this domain contains the possible interaction region. Biotin labeled lamin tail fusion proteins have been produced to be used in further assays. Plans have been detailed for using this data for future experiments.