Dr. Michael C. Yu
Biological Functions of Protein Methylation
Ph.D. 2001 University of California,
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: email@example.com
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.
Moore, MJ, Schwartzfarb, E.M., Silver, P.A. And M.C. Yu (2006) "Differential Recruitment of the Splicing Machinery during Transcription Predicts Genome-Wide Patterns of mRNA splicing" Manuscript accepted for publication in Molecular Cell.
Yu, M.C., Lamming, D.W., Eskin, J.A., Sinclair, D.A., and Silver, P.A. (2006) "The Role of Protein Arginine Methylation in the Formation of Silent Chromatin" Genes & Dev. 20(23):3249-3254
Tsankov, A., Brown, C.R., Yu, M.C., Win, M., Silver, P.A., and Casolari, J.M. (2006) Communication between levels of transcriptional control improves robustness and adaptivity Mol Syst Biol. 2:65
Yu, M.C., Bachand, F.,
McBride, A.E., Komili, S., Casolari, J.M., and Silver,
P.A. (2004) Arginine methyltransferase affects
interaction and recruitment of mRNA processing and export
factors Genes & Dev. 18(16):2024-35
(see News and Views in Nature Structural & Molecular Biology, Oct. 2004 11(10):914-5)
Hieronymus, H., Yu, M.C., and Silver, P.A. (2004) mRNA Surveillance is Coupled to mRNA export Genes & Dev. 18(21):2652-62.
Yu, M.C., Orlando, T.C., Sturm, N.R., Zhou, L., Saito, R.M., Floeter-Winter, L.M. and Campbell, D.A. (2002) Two distinct functional spliced leader RNA gene arrays in Leishmania tarentolae are found in several lizard Leishmania species Int. J. Parasitol. 32(11):1411-22
Yu, M.C., Roberts, T.G., Sturm, N.R., and Campbell, D.A. (2000) In vitro transcription of mutated Leishmania tarentolae spliced leader RNA genes approximates in vivo patterns Mol. Bioch. Parasitol. 111:391-9