Date of Completion

Summer 6-8-2021

Thesis Advisor(s)

Kenneth Campellone

Honors Major

Molecular and Cell Biology

Disciplines

Amino Acids, Peptides, and Proteins | Biochemistry | Biological Phenomena, Cell Phenomena, and Immunity | Cellular and Molecular Physiology | Chemical and Pharmacologic Phenomena | Medical Cell Biology | Medical Pharmacology | Molecular Biology | Molecular Genetics | Pharmaceutical Preparations

Abstract

Parkinson's Disease (PD) is a progressive neurodegenerative and movement disorder primarily caused by the degradation of dopaminergic neurons. Known markers of neurodegeneration in PD are Lewy Bodies, which are fibrillar aggregates that are found in the brains of PD patients. Lewy Bodies can accumulate from specific mutations in the SNCA gene that codes for alpha-synuclein, a protein enriched in presynaptic neurons. A mutated SNCA gene can cause conformational aggregates of alpha-synuclein to form toxic species mediating neuronal death. Research into alpha-synuclein has led to the discovery of a binding partner known as synphilin-1 that is also found in protein aggregates including Lewy Bodies in neurons of PD patients. Proteasomal pathways and autophagy are known to control the degradation of alpha-synuclein and synphilin-1 to moderate this cellular toxicity. How the cytosolic inclusions of synphilin-1 and alpha-synuclein are related to changes in the degradation of these proteins is debated. Furthermore, little is known about the physiological function of synphilin-1 or its role in pathogenesis. This literature review will synthesize existing research regarding synphilin-1’s role in degradative pathways and establish future avenues for research.

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