School of Science Division of Life Science 18 Analysis of Surface Delivery of Epidermal Growth Factor Receptors Supervisor: GUO Yusong / LIFS Student: LI Sui Ki / BIOT Course: UROP 1000, Summer This study investigated the physiological effects of the Ser249Cys mutation in the FGFR3 gene, focusing on protein expression and cellular changes. Using site-directed mutagenesis, PCR amplification, and bacterial transformation, we generated mutated FGFR3 plasmids and transfected them into astrocytes. Immunofluorescence staining revealed detectable but weak pFGFR3 (phospho Y724) signals across samples (Clone 1,2,3), with clone 2 showing the highest expression. The HA tag confirmed specificity, while controls validated antibody efficacy. The findings suggest modest pFGFR3 secretion, possibly due to inefficient phosphorylation or rapid turnover. Astrocytes exhibited lower transfection viability than HeLa cells, likely due to lipofection-induced stress. These results contribute to understanding FGFR3 mutation impacts in skeletal disorders and oncology, supporting future therapeutic research. Analysis of Surface Delivery of Epidermal Growth Factor Receptors Supervisor: GUO Yusong / LIFS Student: PARK Taejun / BCB Course: UROP 1000, Summer SorLA, an intracellular sorting receptor for cargo proteins (e.g., kinases/phosphatases), is highly related to Alzheimer’s disease (AD) when dysfunctional (Schmidt). The implication of SorLA to AD relies on its ability to sort the Amyloid precursor protein (PP) and regulate the disruptive Aβ (beta-amyloid) formation. Additionally, SorLA also plays an important part in the endosomal-lysosomal system due to its sorting or binding ability to many other cargo clients or adaptors. Thus, a deeper understanding of SorLA may advance Alzheimer’s therapeutics and shed more light on its overall regulatory role especially in the neuronal system. Zhou Peizhi, my student mentor, has previously discovered that SorLA knocked out (KO) HEK293T cell line caused CI-MPR mis-trafficking along with lysosomal functional defects. It has been previously reported that the retromer complex can bind both to CI-MPR and SorLA by its VPS35 and VPS26 subunit, respectively. We hypothesize that disrupted SorLA-retromer binding impairs retromer function, causing CI-MPR mistrafficking. In this UROP study, we decided to closely examine this hypothesis and the mechanism of lysosomal defects caused in SorLA KO cell lines. Functional Roles of Arfpr1 in Regulating Export of Cargo Proteins out of the Trans Golgi Network Supervisor: GUO Yusong / LIFS Student: CHOI Kin Long Ryan / BIBU Course: UROP 1100, Spring The Epidermal Growth Factor Receptor EGFR is a receptor which binds with EGF on the cell surface. Upon binding, signals will be sent to the cell for cell proliferation and migration, making it a crucial substance in our cells. The EGFR is initially synthesized in the endoplasmic reticulum ER then transported to the Golgi, lastly arriving at the cell membrane for activation.
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