Brief Communication abstract
Nature Cell Biology 8, 894 - 896 (2006)
Published online: 9 July 2006 | doi:10.1038/ncb1450
A 
-secretase-like intramembrane cleavage of TNF
by the GxGD aspartyl protease SPPL2b
Regina Fluhrer1, Gudula Grammer1, Lars Israel2, Margaret M. Condron3, Christof Haffner1, Elena Friedmann4, Claudia Böhland1, Axel Imhof2, Bruno Martoglio4,5, David B. Teplow3 & Christian Haass1
-secretase and signal peptide peptidase (SPP) are unusual GxGD aspartyl proteases, which mediate intramembrane proteolysis. In addition to SPP, a family of SPP-like proteins (SPPLs) of unknown function has been identified. We demonstrate that SPPL2b utilizes multiple intramembrane cleavages to liberate the intracellular domain of tumor necrosis factor 
(TNF) into the cytosol and the carboxy-terminal counterpart into the extracellular space. These findings suggest common principles for regulated intramembrane proteolysis by GxGD aspartyl proteases.
- Adolf Butenandt Institute, Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig Maximilians University, 80336 Munich, Germany.
- Adolf Butenandt Institute, Protein Analysis Unit, Ludwig Maximilians University, 80336 Munich, Germany.
- Department of Neurology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
- Swiss Federal Institute of Technology, ETH Hoenggerberg, 8092 Zurich, Switzerland.
- Present address: Expertise Platform Proteases, Novartis Institutes for Biomedical Research, Novartis Pharma AG, 4002 Basel, Switzerland.
Correspondence to: Christian Haass1 e-mail: chaass@med.uni-muenchen.de
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