Author: ["Regina Fluhrer","Gudula Grammer","Lars Israel","Margaret M. Condron","Christof Haffner","Elena Friedmann","Claudia Böhland","Axel Imhof","Bruno Martoglio","David B. Teplow","Christian Haass"]
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Abstract
γ-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 α (TNFα) 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.Cite this article
Fluhrer, R., Grammer, G., Israel, L. et al. A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b. Nat Cell Biol 8, 894–896 (2006). https://doi.org/10.1038/ncb1450 