Presenter Information

Madeline GanshertFollow

Major

Biology

Anticipated Graduation Year

2025

Access Type

Restricted Access

Abstract

Phosducin-like proteins (PhLPs) are highly conserved among eukaryotes from yeast to humans. Although their biological function is unclear, it is hypothesized that they are involved in microtubule assembly and folding. Here I investigate the potential PhLP-3 association with microtubules. To study this, I used immunofluorescence assays and confocal microscopy to determine the subcellular localization of PhLP-3 in the human U2OS cell line. My results show diffuse localization of PhLP-3 throughout the cytosol, indicating that the protein does not associate with microtubules. Our next step is determining whether PhLP-3 co-localized with cytosolic chaperone CCT, which facilitates tubulin folding.

Faculty Mentors & Instructors

Stefan Kanzok, Associate Professor, Department of Biology

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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Investigating the Association of Phosducin-like Protein 3 (PhLP-3) to Microtubules in a Cell Culture System

Phosducin-like proteins (PhLPs) are highly conserved among eukaryotes from yeast to humans. Although their biological function is unclear, it is hypothesized that they are involved in microtubule assembly and folding. Here I investigate the potential PhLP-3 association with microtubules. To study this, I used immunofluorescence assays and confocal microscopy to determine the subcellular localization of PhLP-3 in the human U2OS cell line. My results show diffuse localization of PhLP-3 throughout the cytosol, indicating that the protein does not associate with microtubules. Our next step is determining whether PhLP-3 co-localized with cytosolic chaperone CCT, which facilitates tubulin folding.