Identification of signal peptide peptidase, a presenilin-type aspartic protease

被引：459

作者：

Weihofen, A

Binns, K

Lemberg, MK

Ashman, K

Martoglio, B ^{[1
]}

机构：

[1] ETH Honggerberg, Swiss Fed Inst Technol, Inst Biochem, CH-8093 Zurich, Switzerland

[2] Samuel Lunenfeld Res Inst, Toronto, ON M5G 1X5, Canada

来源：

SCIENCE | 2002年 / 296卷 / 5576期

关键词：

D O I：

10.1126/science.1070925

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans, SPP activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. We have identified human SPP as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. SPP and potential eukaryotic homologs may represent another family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides.

引用

页码：2215 / 2218

页数：5

共 24 条

[1]

Brachmann CB, 1998, YEAST, V14, P115

[2] HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C [J].