Honors College Thesis
 

Characterization of Fer1L6 in the mouse C2C12 cell line

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  • Fer1L6 is an uncharacterized member of the ferlin family of proteins, a group of large, calcium sensitive proteins with emerging roles in vesicle trafficking and various disease states. The presence of Fer1L6 has been identified within the C2C12 cell line of mouse skeletal muscle. To determine the protein’s subcellular location within the cell, we used immunofluorescence. Results indicated Fer1L6 localized to the plasma membrane and perinuclear region, specifically at lamellopodia and adhesion junctions. Co-immunofluoresence, proximity ligation, and co-immunoprecipitation experiments were then performed to identify any Fer1L6 binding partners so as to aid in elucidating the protein’s function. The proteins syntaxin-4, SNAP-23, vimentin, and actin were confirmed to bind Fer1L6. Additionally, the focal adhesion proteins vinculin and talin-1, were observed to be in close proximity to Fer1L6. This suggests that Fer1L6 may play a role in vesicle trafficking and membrane fusion at focal adhesions. Thus, Fer1L6 may function as a regulator in the recycling of the focal adhesion complex.
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