Protein Degradation: Accumulation and Localization of GLR-1 in absence of E3 ligase HRDL-1

All living organisms have mechanisms in place to maintain favorable internal conditions. Proteins, the molecular machinery of the cell, are subject to one of these mechanisms called endoplasmic reticulum associated degradation (ERAD), in which misfolded or damaged proteins are destroyed. In ERAD, E3 ligases add ubiquitin to damaged proteins, which are then removed via degradation. When ERAD is non-functional, it could be a contributing factor to diseases like Alzheimer's and Parkinson's. Our lab has collected evidence that the E3 ligase HRDL-1 ubiquitinates GLR-1, a glutamate receptor protein in neurons that functions in the locomotion of Caenorhabditis elegans. In the absence of HRDL-1, evidence suggests that GLR-1 builds up in neuron cells, but no data has been collected to specify where the buildup of protein occurs on an organelle level. In our experiment, we attempt to characterize GLR-1 accumulation when HRDL-1 is not present.