Abstract

FAM171B is a relatively uncharacterized protein that contains fourteen consecutive glutamine residues within its primary amino acid sequence; thus it is a polyglutamine (polyQ) protein. PolyQ proteins are interesting because mutations within the polyQ tract have been linked to a number of severe neurodegenerative diseases including Huntingtons Disease (HD). To date, there are minimal published data regarding FAM171B and its molecular function, such that both expression levels and intracellular localization have yet to be definitively determined. Using immunohistochemical and in situ hybridization analyses, our lab has recently found that FAM171B is expressed throughout the mouse brain. This current study attempts to build off this information to identify the intracellular localization of FAM171B in several different nervous system cell types including: a human glioblastoma cell line (U138), a human neuroblastoma cell line (SH-SY5Y), and mouse brain primary neurons. Using immunofluorescence, FAM171B-GFP fusion proteins, and live cell imaging (coupled with confocal microscopy) our data indicate that FAM171B has a predominantly vesicular/punctate staining within the cytoplasm of cells. Furthermore, colocalization studies using organelle specific markers shows that FAM171B localizes to both endosomes and cellular regions near the plasma membrane. Taken together, our data suggests that FAM171B may play a vesicle trafficking role within cells of the nervous system.

Advisor

Geoffrey Goellner

Committee Member

David Sharlin

Committee Member

Rachel Cohen

Date of Degree

2020

Language

english

Document Type

Thesis

Degree

Master of Science (MS)

Department

Biological Sciences

College

Science, Engineering and Technology

Creative Commons License

Creative Commons Attribution-Noncommercial 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License

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