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Full-Text Articles in Life Sciences
Investigating The Role Of Er-Associated Degradation In An Olfactory Neuron In The Nematode, Caenorhabditis Elegans, Heino Hulsey-Vincent
Investigating The Role Of Er-Associated Degradation In An Olfactory Neuron In The Nematode, Caenorhabditis Elegans, Heino Hulsey-Vincent
WWU Graduate School Collection
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 …
Regulation Of Glutamate Receptor (Glr-1) Under Endoplasmic Reticulum Stress In Caenorhabditis Elegans, Janie Aguilera
Regulation Of Glutamate Receptor (Glr-1) Under Endoplasmic Reticulum Stress In Caenorhabditis Elegans, Janie Aguilera
WWU Graduate School Collection
Neurons communicate with other cells to elicit outputs that include memory and movement. Cells, including neurons, create proteins every day for specific functions and in particular, neurons produce proteins that enable their communication. Proteins found in cellular membranes are synthesized at the endoplasmic reticulum (ER). However, up to 30% of new proteins are improperly folded and must be removed from the cell. A build-up of misfolded proteins can trigger the Unfolded Protein Response (UPR) which initiates other pathways of protein quality control and can determine the fate of a cell. ER-associated protein degradation (ERAD) is a ubiquitin-dependent process in eukaryotic …
Roles Of Ubiquitin And Stress In Diacetyl Chemosensation Of C. Elegans, Ellen Zocher, Nelson Ruth, Marissa Hogg
Roles Of Ubiquitin And Stress In Diacetyl Chemosensation Of C. Elegans, Ellen Zocher, Nelson Ruth, Marissa Hogg
Scholars Week
Ubiquitin is a small protein that can be attached to other proteins in a cell, tagging them for destruction. The process of adding ubiquitin to a protein substrate (ubiquitination), and the subsequent trafficking and degradation of this substrate, is a principle regulator of the abundance and activity of many proteins across all forms of life. We are examining the role and dynamics of this regulatory system in the olfactory neurons of the model organism Caenorhabditis elegans, specifically the olfactory receptor protein ODR-10, which allows the worm to detect diacetyl, a volatile compound that is produced by the bacteria the worm …
Regulation Of Ampa-Type Glutamate Receptor Homolog Glr-1 By Erad Ubiquitin Ligases In C. Elegans, Sam Witus
Regulation Of Ampa-Type Glutamate Receptor Homolog Glr-1 By Erad Ubiquitin Ligases In C. Elegans, Sam Witus
Scholars Week
Endoplasmic reticulum-associated degradation (ERAD) maintains cellular health by removing misfolded proteins from the endoplasmic reticulum (ER). ERAD is ubiquitin-dependent, and ubiquitination of target proteins can be catalyzed by ER-resident E3 ubiquitin ligases. In C. elegans, genes for three putative ERAD E3 ubiquitin ligases have been identified: hrd-1, hrdl-1, and marc-6 (HRD-1, GP78/AMFR, and MARCH-6 in mammalian systems). In C. elegans, these three genes cooperate to maintain the overall health of animals during ER stress. We are testing the roles of hrd-1, hrdl-1, and marc-6 in the neurons of C. elegans. GLR-1 is a glutamate receptor that is expressed in a …
Importance Of Ubiquitin-Mediated Degradation On Diacetyl Chemosensation In C. Elegans, Ellen Zocher, Nelson Ruth
Importance Of Ubiquitin-Mediated Degradation On Diacetyl Chemosensation In C. Elegans, Ellen Zocher, Nelson Ruth
Scholars Week
Ubiquitin is a small regulatory protein that can be attached to other proteins in a cell, tagging them for destruction. Ubiquitin plays a critical role in regulating the abundance and activity of many proteins. We examined the role of ubiquitin and the cellular pathway it follows in olfactory neurons in the model organism C. elegans. C. elegans senses and moves towards sources of diacetyl, a volatile compound generated by the bacteria it consumes. This behavior is dependent on the diacetyl receptor, ODR-10. We hypothesized that the ubiquitin-mediated degradation system is involved in the regulation of this sensory receptor. Using transgenic …