Dr. Michael C. Yu

Biological Functions of Protein Methylation

Assistant Professor

Ph.D. 2001 University of California, Los Angeles
NIH Post-doctoral Fellow 2002-2005 Harvard Medical School

Assistant Professor 2006 SUNY-Buffalo

Address Information

Michael Yu
Department of Biological Sciences
355 Cooke Hall
State University of New York at Buffalo
Buffalo, NY 14260

(716) 645-2363 ext: 135

To send e-mail: mcyu@buffalo.edu


A majority of cellular proteins undergo post-translational modifications. The purpose of these modifications is to serve as cellular molecular switches and to increase proteomic repertoire of a cell. Recently, protein arginine methylation has emerged as a major regulator of protein function. This modification is catalyzed by a family of evolutionarily conserved enzyme called protein arginine methyltransferase (PRMT). In mammalian cells, nine PRMTs and a number of in vivo substrates have been identified thus far. In metazoans, arginine methylation has been shown to be important in the differentiation and development as well as human diseases such as multiple sclerosis, spinal muscular atrophy, and cancer. At the cellular level, this modification affects intracellular protein transport, signal transduction, RNA-processing, and transcription.

Using both yeast and mammalian cells as model organisms, my lab is focused on understanding the biological functions of protein arginine methylation at the molecular level using cell biological, biochemistry, and genomics approaches. We are also interested in developing high-throughput technologies that will allow us to rapidly screen and identify PRMT substrates.