Date of Award

Summer 8-15-2026

Degree Type

Thesis

Degree Name

MS Biology

Department

Biology

Advisor

C.J. Urso, Ph.D

Committee Member

Edward G. Tall, Ph.D

Committee Member

Katherine Varandas, Ph.D

Keywords

depalmitoylation, neuroblastoma cells, neuronal differentiation, palmitoylation, post-translational modifications, retinoic acid, SH-SY5Y cell

Abstract

Palmitoylation is a reversible post-translational modification involving covalent attachment of palmitoyl groups to cysteine residues. Till date, 23 members of this family have been identified in mammals, located in Golgi apparatus and endoplasmic reticulum and nearly 40% of synaptic proteins are estimated undergo palmitoylation. These proteins include vesicle fusion proteins (SNARE), signaling molecules, ion channels and neurotransmitter receptors such as gamma-aminobutyric acidreceptors, kainate receptors and glutamate receptors. While its role in neuronal function has been widely recognized, comparatively little is known about how depalmitoylation-associated enzymes are regulated during neuronal differentiation. The present study aimed to characterize changes in depalmitoylation-associated gene expression during retinoic acid (RA)-induced differentiation of SH-SY5Y neuroblastoma cells and to evaluate the functional relationships among these proteins using bioinformatics analyses. The SH-SY5Y human neuroblastoma cell line is widely used as an in-vitromodel of neuronal differentiation. These cells were differentiated for seven days and neuronaldifferentiation was confirmed through quantitative assessment of neurite morphology. Gene expression was evaluated using quantitative real-time PCR, followed by protein-protein interaction network construction using STRING, hub protein identification with Cytoscape/cytoHubba and functionalenrichment analysis using g:Profiler. RA treatment induced marked morphological differentiation with significant neurite remodeling. qPCR analysis demonstrated selective changes in depalmitoylation-associated gene expression, including significant upregulation of ABHD13 and downregulation of APT2 (LYPLA2), whereas the remaining genes showed relatively limited transcriptional changes. Network analysis identified ABHD10 and ABHD17A as consistently central hub proteins and enrichment analysis

linked the gene set to depalmitoylation, neuronal organization, synaptic function and protein localization.

Together, these findings indicate that neuronal differentiation is associated with selective transcriptional changes within the depalmitoylation machinery while also highlighting the importance of protein interaction networks in identifying key regulatory candidates. This study provides a foundation forfuture investigations into the functional roles of depalmitoylation during neuronal differentiation and neurodegenerative disease.

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