Effects of ERAD E3 ligase mutations on C. elegans food seeking behavior

Endoplasmic Reticulum Associated Degradation (ERAD) is a cellular process that prevents protein aggregation by tagging misfolded proteins with ubiquitin at the endoplasmic reticulum (ER), marking them for destruction (figure 1) (7,6,5). E3 ubiquitin ligases participate in the ubiquination process of target proteins during ERAD (figure 1) (7,6,5). Protein aggregation is important to study because it is seen in neurodegenerative disorders such as Alzheimer's and Parkinson's disease (7). In order to research how ERAD works to prevent protein aggregation, a model protein, GLR-1, is used for this research. GLR-1 is required for food seeking behaviors in the microscopic worm, C. elegans (3). In order to understand what interactions GLR-1 may have with each of the E3 ligases that are involved in the ERAD pathway, the food seeking behavior of three different C. elegans strains that each have one mutated, non-functional E3 ligase, hrdl-1, hrd-1 and marc-6, were tested and compared.