Lowe, Troy
Troy is in the Biochemistry, Molecular and Structural Biology Graduate Program and joined the CMB training program in 2018. He received his B.S and M.S degrees in Biochemistry from San Francisco State University.
Mentor: Dr. Steven Clarke
Posttranslational modifications have been of huge interest in the past decade, the modifications of proteins that correlate with disease-related phenotypes in particular. One modification that has gained a significant spotlight is methylation and the role it plays as a genetic marker involved with transcriptional silencing, cancer cell proliferation, and intracellular signaling. Currently, nine human protein arginine methyltransferase (PRMTs) have been identified, yet much about the mechanism, regulation, and purpose of these methyltransferases remain unclear. Just as the name of the enzyme states, PRMTs catalyze the methylation of the guanidino side chain of arginine and are classified into three types. The type I PRMTs that catalyze the addition of asymmetric dimethylation as a final product are PRMT1, PRMT2, PRMT3, PRMT4, PRMT6, and PRMT8. The type II PRMTs that catalyze the addition of symmetric dimethylation as a final product are PRMT5 and PRMT9. The one type III PRMT that catalyzes only monomethylated products is PRMT7.
My research involves understanding the biological role of PRMT7 and the involvement it has with cancer metastasis. Currently, our lab is studying how small molecule inhibitors interact with this enzyme, including SAM analogs like methylthioladenosine, peptide inhibitors like EPZ015666, and potential bisubstrate inhibitors EML 709, 734, and 736. In addition to understanding these inhibitors, my interests involve understanding the physiological effect of temperature, pH, and ionic conditions on PRMT7 expression and activity. These studies will ultimately shed light on potential therapeutic treatments to control cancer metastasis, and help understand how methylation regulates genetic transcription.
