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Abstract

The phosphorylation of Growth Associated Protein may affect the rate of interaction between GAP-43 and the Amyloid Precursor Protein. By synthesizing mutants of the GAP-43 protein, the amount of C-terminal fragments of APP that results from the interaction could be observed under various conditions. The two mutants, S41A and S41D, and the wild type GAP-43 were both co-expressed with APP in moues neuroblastoma cells and analyzed on a Western blot. The mutant used to block phosphorylation showed a greater rate of interaction with APP, while the mutant that was created to mimic the effect of phosphorylation showed less interaction. Further study of this research would include verifying the interaction of the two proteins through a co-immunoprecipitation experiment and determining the mechanism by which GAP-43 mediates changes in APP metabolism.

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