A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b

被引：122

作者：

Fluhrer, Regina

Grammer, Gudula

Israel, Lars

Condron, Margaret M.

Haffner, Christof

Friedmann, Elena

Boehland, Claudia

Imhof, Axel

Martoglio, Bruno

Teplow, David B.

Haass, Christian ^{[1
]}

机构：

[1] Univ Munich, Adolf Butenandt Inst, Dept Biochem, Lab Alzheimers & Parkinsons Dis Res, D-80336 Munich, Germany

[2] Univ Munich, Adolf Butenandt Inst, Prot Anal Unit, D-80336 Munich, Germany

[3] Univ Calif Los Angeles, Dept Neurol, David Geffen Sch Med, Los Angeles, CA 90095 USA

[4] ETH Honggerberg, Swiss Fed Inst Technol, CH-8092 Zurich, Switzerland

来源：

NATURE CELL BIOLOGY | 2006年 / 8卷 / 08期

关键词：

D O I：

10.1038/ncb1450

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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 ( TNF alpha) 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.

引用

页码：894 / U175

页数：6

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