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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 …