δ-catenin plays an integral role in neural communication and has been shown to affect cognitive function when

mutated or insufficiently expressed. Inadequate amounts of δ-catenin present between synapses during

neurodevelopment has been linked to Cri-du-Chat syndrome, Alzheimer’s disease, and specific forms of autism. To

further elucidate the processes by which δ-catenin expression is inhibited, our research genetically manipulates

segments of the δ-catenin mRNA – more specifically, the 5’ untranslated region (5’UTR), coding sequence (CDS),

and 3’ untranslated region (3’UTR) – to examine how molecular structure may regulate protein production. Each

segment is incorporated in plasmids alongside a fluorescent reporter that allows us to visualize produced protein

upon introducing the DNA in mouse primary cells. By photobleaching the primary cells prior to temporal analysis,

we are able to detect the amount of new protein produced through fluorescence microscopy. We expect that, in cell

cultures containing the 5’UTR mutation, non-specific ribosomal proteins may bind to the hairpin structure of the

sequence, causing lessened δ-catenin expression over time. Interactions with microRNAs present in the cytoplasm

by the 3’UTR may degrade expression at a greater extent than the 5’UTR. Thoroughly understanding these effects

on δ-catenin production will ultimately aid in the development of neurological pharmaceuticals at a molecular level.