Date of Completion
Honors College Thesis
DCBLD2 is a scaffolding receptor possibly involved in neuronal migration or differentiation. It contains seven intracellular tyrosine sites that can be phosphorylated to allow Crk/CrkL binding. Crk/CrkL are involved in the Reelin signaling pathway that regulates neuronal migration in the developing cortex. My research was aimed at understanding the subcellular localization of DCBLD2 and to determine if its ability to become tyrosine phosphorylated altered its localization. I hypothesized that DCBLD2 would localize similarly to NP1 and PlxnA2 based on their similar functions relayed to axon guidance and their similar ectodomains. DCBLD2 is termed a neuropilin-like protein as they have similar ectodomains. NP1 is a co-receptor to PlxnA2 and together they respond to semaphorins to regulate axonal guidance. Therefore, DCBLD2 might localize similarly to NP-1 and PlxnA2 within a cell. It is possible that the mutant version of DCBLD2, lacking the seven tyrosine sites, will localize differently than the wild type, perhaps driving it more or less towards the plasma membrane. I created three constructs to study DCBLD2 in human embryonic kidney cells. These constructs were visualized via immunofluorescence. From the images and statistical results, both DCBLD2 wild type and the phosphorylation site mutant localize similarly to PlxnA2.
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Bullock, Sarah A., "Characterization of the Subcellular Localization of DCBLD2 and its Regulation by Tyrosine Phosphorylation" (2017). UVM Honors College Senior Theses. 449.