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Neurons use electrical and chemical signals to communicate with each other at gaps called synapses. Synapses must form correctly during nervous system development, or neurological diseases such as schizophrenia, Tourette syndrome, and OCD can result. Adhesion proteins like Slitrk2 are located in the postsynaptic cell membrane, where they direct axons to form synapses at the correct locations. Trans-synaptic binding partners for Slitrk2 have already been identified, but not much is known about the intracellular binding partners of Slitrk2. Previous studies in our lab used biochemical assays to identify PSD-95 as an intracellular binding partner of Slitrk2. PSD-95 are scaffolding proteins that have important roles in postsynaptic organization at excitatory synapses. To see if Slitrk2 and PSD-95 colocalize at neuronal synapses, embryonic mouse forebrains were dissected and dissociated, and the neurons were cultured for two weeks. Then, immunocytochemistry was used to stain for endogenous Slitrk2 and PSD-95 proteins in cultured cortical neurons. Through the use of primary and secondary antibodies to mark these proteins of interest, a colocalization between Slitrk2 and PSD-95 was observed. In contrast, when Slitrk2 was co-stained with gephyrin, a known inhibitory synapse marker, no overlap was observed. We are currently working on an accurate method for quantifying the degree of colocalization between slitrk2 and PSD-95 at neuronal synapses.
Stephens, Aliyah, "The Potential Colocalization of Slitrk2 and PSD-95 at Neuronal Synapses" (2018). Neuroscience Summer Fellows. 11.
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