Faculty Mentor(s)
Dr. Leah Chase, Biology and Chemistry
Document Type
Poster
Event Date
4-12-2024
Abstract
Membrane protein xCT and its heavy chain component 4F2HC make up the xc- transport system. 4F2HC may be necessary for membrane localization of the heterodimer and xCT is responsible for transport activity. Under basal conditions, xCT resides in endosomes, but upon oxidative insult, xCT moves to the membrane and functions to reduce oxidative stress. We hypothesize the movement of xCT to the membrane is directed by changes in posttranslational modifications (PTMs) such as phosphorylation, ubiquitination and glycosylation. The overall goal of this project is to use mass spectrometry to detect the PTMs of xCT isolated from cells grown under basal conditions and those exposed to oxidative stress. Currently we have found significant coverage of the C-terminus and intermembrane regions of xCT and sites of phosphorylation and oxidation. Future plans are to identify peptides covering the N-terminus of xCT. We have also identified co-expressed 4F2HC peptides in our samples, and we will be prioritizing its coverage in future analyses.
Recommended Citation
Repository citation: Bricco, Connor, "LC-MS/MS for Proteomic Analysis of Post-translational Modifications on xCT" (2024). 23rd Annual A. Paul and Carol C. Schaap Celebration of Undergraduate Research and Creative Activity (2024). Paper 10.
https://digitalcommons.hope.edu/curca_23/10
April 12, 2024. Copyright © 2024 Hope College, Holland, Michigan.
Comments
This research was supported by the Thomas L. Riechel Endowed Fund for Summer Research in Chemistry and the Schaap Science Undergraduate Research Fund.