Open Access. Powered by Scholars. Published by Universities.®

Life Sciences Commons

Open Access. Powered by Scholars. Published by Universities.®

Biology

Scholars Week

Conference

C. elegans

Publication Year

Articles 1 - 3 of 3

Full-Text Articles in Life Sciences

Roles Of Ubiquitin And Stress In Diacetyl Chemosensation Of C. Elegans, Ellen Zocher, Nelson Ruth, Marissa Hogg May 2016

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 May 2016

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 May 2015

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 …