IDENTIFICATION OF TNFAIP8L1 BINDING PARTNERS THROUGH CO- IMMUNOPRECIPITATION AND MASS SPECTROMETRY
Author: Audrey Hoyle
Major: Biochemistry & Microbiology
Graduation Year: 2018
Thesis Advisor: Con Sullivan
Description of Publication: The expanded understanding of the gene families and mechanisms governing tumorigenesis pathways has enormous potential for improving current cancer therapies and patient prognoses. One such gene family that participates in the regulation of tumorigenesis is the tumor necrosis factor alpha-induced protein 8 (TNFAIP8) gene family, which is comprised of four members: TNFAIP8, TNFAIP8L1, TNFAIP8L2, and TNFAIP8L3. The TNFAIP8L1 gene is thought to function as a tumor suppressor, but the mechanisms by which it exerts this function have yet to be elucidated. We hypothesize that the TNFAIP8L1 protein acts as a tumor suppressor through protein-protein interactions that regulate tumor proliferation, migration, and/or angiogenesis. The H1299 non-small cell lung cancer cell line was engineered to overexpress TNFAIP8L1 protein and is being used as an in vitro model to identify putative protein binding partners through co-immunoprecipitation and mass spectrometry assays. Apparent interactions will be validated by mammalian two-hybrid assays. We anticipated that TNFAIP8L1 would bind proteins involved in tumorigenesis pathways and that these may reveal new avenues of study and hold important clinical relevance in current cancer treatment plans. We identified 138 putative protein interactions involving TNFAIP8L1.
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URL to Thesis: https://digitalcommons.library.umaine.edu/honors/335