Research Mentor(s)
Dahlberg, Lina
Description
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 strains with dysfunctional ubquitin-mediated degredation systems in their olfactory neurons, we studied how mutant strains of C. elegans react to diacetyl, and visualized their ODR-10 levels through fluorescence imaging. Our preliminary results suggest that overexpression of ubiquitin is detrimental to the olfactory sensation of diacetyl in C. elegans.
Document Type
Event
Start Date
14-5-2015 10:00 AM
End Date
14-5-2015 2:00 PM
Department
Biology
Genre/Form
student projects; posters
Subjects – Topical (LCSH)
Caenorhabditis elegans; Ubiquitin; Protein folding; Proteins--Metabolism; Proteins--Pathophysiology
Type
Image
Keywords
Caenorhabditis elegans, C. elegans, Cell, Receptor, ODR-10, Ubiquitin, Transgenic, Fluorescence imaging, Chemotaxis
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this documentation for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.
Language
English
Format
application/pdf
Included in
Importance of ubiquitin-mediated degradation on diacetyl chemosensation in c. elegans
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 strains with dysfunctional ubquitin-mediated degredation systems in their olfactory neurons, we studied how mutant strains of C. elegans react to diacetyl, and visualized their ODR-10 levels through fluorescence imaging. Our preliminary results suggest that overexpression of ubiquitin is detrimental to the olfactory sensation of diacetyl in C. elegans.