Life Sciences Commons^™

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 …

Evidence For Secretion Of A Netrin-1-Like Protein By Tetrahymena Thermophila, Victoria E. Ames, Grant Hooper, Aubrey J. Juris, Cole Knox, Jack Lightbody, Alexa C. Manthei, Jacob P. Olejarczyk, Benjamin D. Swenor, Amiah Warder, Emily B. Weindorf, Taylor L. Vander Plas, Heather G. Kuruvilla

The Research and Scholarship Symposium (2013-2019)

Netrin-1 is a pleiotropic signaling molecule with targets in many mammalian cell types. Though first characterized as a chemotactic signal involved in neuronal guidance during development, netrin-1 has since been found to have a regulatory role in angiogenesis, and is also used as a biomarker in certain cancers.

Tetrahymena thermophila are free-living protists that rely on chemotactic signals to find food, as well as to escape predators. Chemoattractants cause the cells to swim faster in the forward direction, while chemorepellents cause ciliary reversal, resulting in movement of the cell away from the noxious stimulus. We have previously found that netrin-1 …