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STEFAN RIEDL, PH.D.
Assistant Professor
Apoptosis and Cell Death Research
858.646.3100x3135 (phone)
858.795.5274 (fax)
sriedl@burnham.org
RESEARCH FOCUS, BIOGRAPHY, STAFF, PUBLICATIONS
Research Focus
All vital cellular functions such as the control of cell proliferation and homeostasis are strictly regulated by distinct pathways. At the very heart of these pathways are protein signaling complexes, which act as switches to orchestrate cell regulation. The goal of Dr. Riedl’s lab is to elucidate the structure and mechanism of these complexes and leverage this knowledge to initiate the search for compounds that combat diseases, such as immune disorders and cancer.
One such signaling complex studied in the Riedl lab is NF-κB- inducing kinase (NIK) in complex with its regulators as a key mediator of NF-κB signaling. Additional regulatory complexes studied involve large signaling platforms such as the death inducing complex (DISC) of the extrinsic apoptotic pathway and the NLR inflammasomes.
Biography
Dr. Riedl studied biochemistry at the University of Bayreuth, Germany and went on to spend the first two years of his doctoral work at the Burnham Institute, La Jolla, California. He received his Ph.D. in the group of Dr. Robert Huber at the Max Planck Institute, Munich, Germany, for his work on the activation and inhibition of caspases. His postdoctoral work on the structure of Apaf-1 was carried out at Princeton University, New Jersey. He joined the faculty of The Burnham Institute for Medical Research as an assistant professor in 2006. His laboratory focuses on the structure and mechanism of signaling platforms and signaling complexes involved in the regulation of cellular pathways.
Selected Publications
Scott FL, Stec B, Pop C, Dobaczewska MK, Lee JJ, Monosov E, Robinson H, Salvesen GS, Schwarzenbacher R, Riedl SJ. The Fas/FADD death domain complex structure unravels signaling by receptor clustering. Nature, In press (2008).
Salvesen, GS, Riedl, SJ. Caspase inhibition, specifically. Structure, 15(5):513-514 (2007).
Riedl SJ, Salvesen, GS. The apoptosome: signaling platform of cell death. Nat. Rev. Mol. Cell. Biol., 8(5):405-413 (2007).
Schimmer AD, Dalili S, Batey RA, Riedl SJ. Targeting XIAP for the treatment of malignancy. Cell Death Differ., 13(2), 179-88 (2006).
Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434,926-33. (2005).
Riedl SJ, Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell. Biol. 5(11),897-907 (2004).
Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS. Structural basis for the inhibition of caspase-3 by XIAP. Cell 104(5):791-800 (2001).
Riedl SJ, Renatus M, Snipas SJ, Salvesen GS. Mechanism-based inactivation of caspases by the apoptotic suppressor p35. Biochemistry 40(44), 13274-80 (2001).
Riedl SJ, Fuentes-Prior P, Renatus M, Kairies N, Krapp S, Huber R, Salvesen GS, Bode W. Structural basis for the activation of human procaspase-7. Proc. Natl. Acad. Sci. USA 98(26),14790-5 (2001).
List of Publications via PubMed
(NIH National Library of Medicine)
