Innate immunity is the first line of defense against invading pathogens in higher eukaryotes. The central players of this well-conserved form of immune response are pattern-recognition receptors (PRRs) that can recognize pathogen associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs). NOD-like receptors (NLRs) are important PRRs of innate immunity. Notably, upon binding PAMP/DAMP and nucleosie-triphosphates (NTP), NLRs assemble into multi-protein complexes called inflammasomes. The assembled inflammasomes then transduce upstream signals to directly activate procaspase-1. The activated caspase-1 then facilitates maturation of inflammatory cytokines via proteolysis. The Sohn Lab asks the following questions: What is the mechanism of inflammasome assembly? What is the mechanism of procaspase-1 activation by inflammasomes? What are the molecular mechanisms of inflammasome regulation by protein modulators?
Lab Website: Jungsan Sohn
Sohn J., Grant, R.A., Sauer, R.T. “Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.” J. Biol. Chem. 2010; 285, 34039-47.
Sohn J., Grant, R.A., Sauer, R.T. “OMP peptides activate the DegS protease by a relief of inhibition mechanism.” Structure. 2009; 17:1411-21.
Sohn J. and Sauer, R.T. “OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations.” Molecular Cell. 2009; 33, 64-74.
Sohn J., Grant R.A., Sauer R.T. “Allosteric activation of DegS, a stress sensor PDZ-protease.” Cell. 2007; 131, 572-583.