Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry

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A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b

Nat Cell Biol 8(8): 894-6

Authors/Editors: Fluhrer R
Grammer G
Israel L
Condron MM
Haffner C
Friedmann E
Bohland C
Imhof A
Martoglio B
Teplow DB
Haass C
Publication Date: 2006
Type of Publication: Journal Article
Gamma-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 alpha (TNFalpha) 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.

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