University of Twente Student Theses


The Effect of α-Synuclein Phosphorylation on the Chaperone Activity of 14-3-3

Han, N.I.C.L. (2023) The Effect of α-Synuclein Phosphorylation on the Chaperone Activity of 14-3-3.

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Abstract:Parkinson’s disease is a neurodegenerative disease, which is believed to be caused by the aggregation of protein α-Synuclein into inclusion bodies in neurons. Cells are able to prevent the formation of cytotoxic aggregates by utilizing cellular protein quality control mechanisms. Protein quality control is regulated by chaperone proteins through the interaction with early aggregates, inhibiting further aggregation. The presence of chaperone protein 14-3-3τ was discovered in α-Syn inclusion bodies, suggesting its potential role in Parkinson’s disease. It has been uncovered that 14-3-3τ specifically binds to phosphorylated serine motifs on proteins. Notably, approximately 90% of the α-Synuclein proteins is phosphorylated in Parkinson’s disease. Building upon these findings, our aim was to investigate whether the chaperone activity of 14-3-3τ is guided by phosphorylation of α-Synuclein. We performed MicroScale Thermophoresis experiments to study the early oligomerization behaviour of α-Synuclein under various conditions. Our findings suggest that 14- 3-3τ ’s chaperone functions are enhanced when α-Syn is phosphorylated. This link between phosphorylation and chaperone activity gives insights into the existing protection mechanisms in cells. Novel understanding of these mechanisms could have implications for the development of effective therapeutic strategies for Parkinson’s disease.
Item Type:Essay (Bachelor)
Faculty:TNW: Science and Technology
Subject:35 chemistry, 42 biology, 44 medicine, 50 technical science in general
Programme:Biomedical Technology BSc (56226)
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