Submission Date

4-24-2023

Document Type

Paper- Restricted to Campus Access

Department

Neuroscience

Adviser

Ellen Dawley

Committee Member

Jennifer King

Committee Member

Samantha Wilner

Department Chair

Carlita Favero

Project Description

Proper synapse formation and maintenance is an important aspect of nervous system development. Errors in synapse formation can cause neurological differences such as schizophrenia, autism, and epilepsy. Slitrks are a family of synaptic adhesion proteins known to induce synapse formation, but little is understood about how they are trafficked or anchored to postsynaptic membrane. Dr. Round’s lab previously discovered that Slitrk2 associates with the intracellular scaffold protein PSD-95, and preliminary data in yeast suggests that a tyrosine residue near the C-terminus of Slitrk2 (Y833) plays a significant role in the interaction. To determine if Y833 mediates the interaction, I generated a version of Slitrk2 in which this tyrosine is mutated to a phenylalanine (Y833F). I then examined the association of Y833F and PSD-95 in Cos-7 cells using coimmunoprecipitation and western blotting. I found that PSD-95 immunoprecipitated equally well with wild-type Slitrk2 and Y833F. These results suggest that Y833, which is a putative phosphorylation site, is not essential for the interaction. Future studies will identify critical residues in Slitrk2 that mediate binding to PSD-95, with the goal of examining the functional significance of the Slitrk2/PSD-95 interaction in neurons.

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