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Date of Award

Winter 2024

Document Type

Masters Thesis

Department or Program Affiliation


Degree Name

Master of Science (MS)



First Advisor

Dahlberg, Lina

Second Advisor

Rose, Jacqueline K.

Third Advisor

Galati, Nick


The breakdown of misfolded proteins is key for cellular health. For proteins at the endoplasmic reticulum (ER), this breakdown is performed through endoplasmic reticulum associated degradation (ERAD). ERAD uses a cascade of E1, E2, and E3 class enzymes to ubiquitylate un- or mis-folded proteins, signaling their destruction. We use the microscopic roundworm Caenorhabditis elegans (C. elegans) as a model organism for studying ERAD. This project investigated the regulation of a neuronal receptor, ODR-10. Our findings suggest that the E2, UBC-6, and the E3, HRDL-1, are required for normal ODR-10 abundance. We worked to uncover whether this regulation is cell autonomous or non-cell autonomous. ODR-10 is solely expressed in the AWA neurons, and the AWA neuron is regulated by the AMsh glial cell. We created rescue strains with transgenes expressing full-length UBC-6 or HRDL-1 in either the AWA neuron, the AMsh glia, or in cells that normally express the gene of interest. We measured the abundance of ODR-10 fused with green fluorescent protein (ODR-10::GFP) in each strain and compared it to ODR-10::GFP levels in a wildtype background. Unexpectedly, the presence of the rescue transgenes caused further disturbance to ODR-10::GFP abundance, and some even changed the shape of the AWA cilia. Our results raise further questions about the role UBC-6 and HRDL-1 may play in neuron-glial interactions, and the mechanism behind ODR-10 regulation.




Protein Quality Control, Endoplasmic Reticulum Associated Degradation, Ubiquitin, Caenorhabditis elegans, Olfactory Receptors


Western Washington University

OCLC Number


Subject – LCSH

Proteolysis; Endoplasmic reticulum; Ubiquitin; Caenorhabditis elegans; Olfactory receptors




masters theses




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Available for download on Saturday, September 14, 2024

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