Investigating Changes in Protein Ubiquitylation Following Sleep Deprivation in Drosophila melanogaster

Student: Koral Kasnyik
Major: Biochemistry and Molecular Biology
Advisors: Dr. Seth Kelly, Dr. William Morgan
Chronic sleep loss is a public health epidemic and is linked to an increased risk of metabolic diseases. Although several models attempt to explain the function of sleep, the molecular mechanisms that link sleep deprivation and disease are unclear. In order to better understand the biological changes that occur following sleep loss, our lab established a fly model of sleep deprivation. Our current data suggests that the ubiquitin proteasome pathway (UPP) may regulate sleep. The UPP functions to tag short-lived or defective proteins with ubiquitin and degrade these proteins via the proteasome complex. Flies were sleep deprived using a variety of methods. Western blot analysis showed that one method resulted in decreased levels of ubiquitylated proteins while alternative methods did not. These results suggest that different methods of sleep deprivation may cause different changes in protein abundance and question whether methods of sleep deprivation can be used interchangeably.

Posted in I.S. Symposium, Independent Study on May 1, 2020.