Member of: The Peter Juo Lab
UFM-1 is a ubiquitin-like molecule that has been implicated in protein quality control, however it is still poorly understood. We previously found that C. elegans mutants defective in UFMylation have increased protein aggregation of a polyglutamine (polyQ40) protein in muscle. CAG trinucleotide repeat diseases like Huntington’s Disease result in expansion of CAG repeats (which codes for glutamine) in specific proteins leading to increased protein aggregation and neurodegeneration with increasing age. Using a variety of approaches, I am investigating the mechanisms by which the UFMylation pathway regulates polyglutamine aggregation in muscle.
BA, Biochemistry & East Asian Studies, Oberlin College, Oberlin, OH