Bachelor of Arts (BA)
Department or Program
Shubhik K. DebBurman
Hongkyun Kim, Rosalind Franklin University of Medicine and Science
SLO-1 is a large conductance potassium channel which when inhibited in C. elegans results in complete ethanol resistance. The protein ERG-28 is responsible for transporting SLO-1 from the endoplasmic reticulum to the golgi apparatus in C. elegans. erg-28 mutants show greatly reduced SLO-1 signaling. We therefore hypothesize that SLO-1 undergoes ER associated degradation via the ubiquitin-proteasome system. We screen for ubiquitin ligase responsible for the degradation of the SLO-1 channel by performing fluorescent microscopy and behavioral studies in C. elegans. The mutants for this ubiquitin ligase showed both increased fluorescence and sensitivity to ethanol. In order to better elucidate the erg-28 and slo-1 pathways we also performed mutagenesis tests on C. elegans with MCHERRY tagged ERG-28. We created multiple mutants expressing a change in fluorescence. These experiments identify different molecules involved SLO-1 signaling pathway.
Haney, James J., "Degradation of SLO-1 BK channels in C. elegans" (2017). Senior Theses.
Available for download on Thursday, May 02, 2019