Hsiu-Ming Shih

Affiliations 

Institute of Biomedical Sciences, Academia Sinica

Biography

Dr. Hsiu-Ming Shih received Ph.D. from University of Minnesota in 1993 and his postdoc training at Vollum Institute in 1996. In 1997, he was appointed as an assistant investigator in National Health Research Institutes and subsequently promoted to be Associate Investigator in 2002. In 2005, he moved to Institute of Biomedical Sciences, Academia Sinica, and became a Full Research Fellow in 2007 and served as a Deputy Director from 2012 to 2014. Dr. Shih is interested in the molecular basis in regulation of sumoylation and ubiquitination associated with human disease. He received numerous awards, including Academia Sinica Young Invesigator Award in 2005, TienTe Lee Biomedical Young Investigator Award in 2007, Academia Investigator Award in 2007, Wang Min-Ning Memorial Award for Outstanding Contribution to the Medical Science and Technology Development, Health and Society in 2013, Distinguished Research Award, National Science Council in 2006, 2010, and 2013.                       

Abstract

Regulation of SUMO binding and Conjugation

Hsiu-Ming Shih

SUMO modification is emerging as an important post-translational control of cellular events. While many SUMO-modified proteins have been identified, little is known about the molecular mechanism underlying SUMO conjugation and binding in response to cellular milieu. Here, we will discuss how phosphorylation modulates SUMO binding and conjugation and show that acetylation of SUMO E2 conjugase Ubc9 selectively down-regulates the sumoylation of substrates with negatively charged amino acid-dependent sumoylation motif. Furthermore, we will demonstrate that acetylation of SUMO-2 at different lysine residues selectively down-regulates the binding of SUMO-2 to different substrates. Structure analyses support differential effects of SUMO acetylation on substrate SIM binding. Some SUMO-2 acetylation in regulation of cell growth and in association with human cancer will be discussed. Altogether, our findings provide the molecular basis underlying phosphorylation and acetylation in modulating selective substrates for SUMO conjugation and binding.