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Post-Translational Modifications of PRL3



Our lab studies the human prenylated protein tyrosine phosphatase PRL3 and its role in promoting metastatic activity in cancer. My project is more specifically focused on the mechanisms of PRL3 regulation. The current work is focused on how the post-translational modification profile of PRL3 impacts a metastatic phenotype.

By over expressing PRL3 in HEK293 cells, we see a shift towards a more oncogenic phenotype (increased proliferation, migration, invasion etc). We are now interested in what happens when we over express mutant PRL3 proteins within a cell. Our mutant PRL3 proteins have been altered to prevent site specific post-translational modifications such and protein modifiers, chemical modifications, and lipid anchors in order to investigate the impact of these modifications on PRL3 activity. We are then able to preform functional assays with the wild type and mutant lines to look for changes in phenotypic output such as the scratch assay.

Post-translational modifications drastically alter the ways in which a protein can function in a cellular environment. By understanding what modifications are controlling PRL3 activity, stability, and trafficking we can begin to have a better understanding of how this phosphatase is modulating oncogenic pathways in the cell.


Trace Jolly is a second year PhD candidate in the Department of Cellular and Molecular Biochemistry.

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