SENP1 Follow-Up
Faculty Mentor Information
Dr. Dinesh Kumar Verma, Boise State University; and Dr. Yonghwan Kim, Boise State University
Presentation Date
7-15-2026
Abstract
SUMOylation is a reversible posttranslational modification in which small ubiquitin-like modifier (SUMO) proteins are covalently attached to lysine residues on target proteins, typically within a consensus motif (ψ–K–X–E). This dynamic process, regulated by SUMO-conjugating enzymes (E1, E2, and E3) and deSUMOylating proteases (SENPs), modulates protein localization, stability, and function. Parkinson’s disease (PD), the second most common progressive neurodegenerative disorder, affects nearly one million individuals in the United States and remains incurable. A pathological hallmark of PD is the aggregation of α-synuclein, which contributes to neuronal degeneration and inflammation. SUMOylation has been reported to increase α-synuclein solubility, suggesting a potential regulatory role in PD pathogenesis. In previous studies, we identified inhibition of SENP1 as a potential therapeutic strategy for PD and identified SSU72, PRKACB, and PSMC5 as candidate proteins regulated by SENP1. In this ongoing study, we aim to validate these findings by assessing the expression and subcellular localization of SSU72, PRKACB, and PSMC5 using Western blotting and Immunocytochemistry (ICC).
SENP1 Follow-Up
SUMOylation is a reversible posttranslational modification in which small ubiquitin-like modifier (SUMO) proteins are covalently attached to lysine residues on target proteins, typically within a consensus motif (ψ–K–X–E). This dynamic process, regulated by SUMO-conjugating enzymes (E1, E2, and E3) and deSUMOylating proteases (SENPs), modulates protein localization, stability, and function. Parkinson’s disease (PD), the second most common progressive neurodegenerative disorder, affects nearly one million individuals in the United States and remains incurable. A pathological hallmark of PD is the aggregation of α-synuclein, which contributes to neuronal degeneration and inflammation. SUMOylation has been reported to increase α-synuclein solubility, suggesting a potential regulatory role in PD pathogenesis. In previous studies, we identified inhibition of SENP1 as a potential therapeutic strategy for PD and identified SSU72, PRKACB, and PSMC5 as candidate proteins regulated by SENP1. In this ongoing study, we aim to validate these findings by assessing the expression and subcellular localization of SSU72, PRKACB, and PSMC5 using Western blotting and Immunocytochemistry (ICC).