Department of biochemistry and Molecular biology
Shaun Olsen, PhD
Biochemistry and Molecular Biology
2013-present Assistant Professor, Medical University of South Carolina, Charleston, SC
2008-2013 Postdoctoral Fellow, Sloan-Kettering Institute, New York, NY
2006-2008 Research Associate, RIKEN Genomic Sciences Center, Yokohama, Japan
2006 PhD, New York University, New York, NY
2000 BA, Rutgers University, New Brunswick, NJ
Office (DDB-206): 843-876-2308
Lab (DDB-220): 843-876-2310
Post-translational modification of proteins by ubiquitin and ubiquitin-like modifiers (collectively termed Ubls) is a means of regulating fundamental cellular processes such as cell cycle control, signal transduction, and differentiation. Ubiquitin conjugation proceeds through the sequential activities of three enzymes (E1, E2, and E3) and alters target protein properties such as activity/conformation, subcellular localization, stability, and capacity for intermolecular interactions, ultimately accounting for the cellular response. The lab aims to understand the molecular mechanisms by which ubiquitin proceeds through its enzymatic cascade and is ultimately conjugated to target proteins in a specific and regulated manner. In addition to its role in maintaining homeostasis, the ubiquitin pathway is implicated in a number of human pathologies including cancer and neurodegenerative disorders and we frame our studies around proteins that when dysregulated are implicated in these disorders. To achieve these goals, we employ a multidisciplinary approach that includes X-ray crystallography complemented with biochemical/biophysical techniques and yeast genetics.
Recent Publications | Additional Publications
Yuan L, Lv Z, Atkison JH, Olsen SK. (2017) Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI. Nat Commun 8:211.
Lv Z, Yuan L, Atkison JH, Aldana-Masangkay G, Chen Y, Olsen SK. (2017) Domain Alternation and Active Site Remodeling Are Conserved Structural Features of Ubiquitin E1. J Biol Chem 292(29):12089-12099.
Lv Z, Rickman KA, Yuan L, Williams K, Selvam SP, Woosley AN, Howe, PH, Ogretmen B, Smogorzewska A, Olsen SK. (2017) S. pombe Uba1-Ubc15 structure reveals a novel regulatory mechanism of ubiquitin E2 activity. Molecular Cell 65(4):699-714.
Atkison JH, Parnham S, Marcotte WR Jr, Olsen SK. (2016) Crystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer Interface. J Biol Chem 291(36):19006-17.
Olsen SK, Lima CD. (2013) Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer. Molecular Cell 49(5):884:96.
Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. (2010) Active site remodeling accompanies thioester bond formation in SUMO E1. Nature 463(7283):906-12.
Lu X, Olsen SK, Capili AD, Cisar JS, Lima CD, Tan DS. (2010) Designed semisynthetic inhibitors of Ub/Ubl E1 activating enzymes. J Am Chem Soc 132(6):1748-9
Olsen SK, Ota N, Kishishita S, Kukimoto-Niino M, Murayama K, Uchiyama H, Toyama M, Terada T, Shirouzu M, Kanagawa O, Yokoyama S. (2007) Crystal structure of the interleukin 15- interleukin 15 receptor alpha complex: insights into trans and cis presentation. J Biol Chem 282(51):37191-204.
Olsen SK, Bromleigh C, Ibrahimi OA, Eliseenkova AV, Zhang F, Linhardt RJ, Joyner AL, Mohammadi, M. (2006) Structural basis by which alternative splicing modulates the biological activity of FGF8 in the brain. Genes Dev 20(2):185-98.