PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8

被引：141

作者：

Ohishi, K ^{[1
]}

Inoue, N ^{[1
]}

Kinoshita, T ^{[1
]}

机构：

[1] Osaka Univ, Microbial Dis Res Inst, Dept Immunoregulat, Suita, Osaka 5650871, Japan

来源：

EMBO JOURNAL | 2001年 / 20卷 / 15期

关键词：

endoplasmic reticulum; glycosylphosphatidylinositol; post-translational modification; transamidase;

D O I：

10.1093/emboj/20.15.4088

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Many eukaryotic cell surface proteins are anchored to the plasma membrane via glycosylphosphatidylinositol (GPI). The GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a preassembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with a substrate protein. It was known that the GPI transamidase is a complex containing GAA1 and GP18. Here, we report two new components of this enzyme: PIG-S and PIG-T. To determine roles for PIG-S and PIG-T, we disrupted these genes in mouse F9 cells by homologous recombination. PIG-S and PIG-T knockout cells were defective in transfer of GPI to proteins, particularly in formation of the carbonyl intermediates. We also demonstrate that PIG-S and PIG-T form a protein complex with GAA1 and GP18, and that PIG-T maintains the complex by stabilizing the expression of GAA1 and GP18. Saccharomyces cerevisiae Gpi16p (YHR188C) and Gpi17p (YDR434W) are orthologues of PIG-T and PIG-S, respectively.

引用

页码：4088 / 4098

页数：11

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