GPI Glycan Remodeling by PGAP5 Regulates Transport of GPI-Anchored Proteins from the ER to the Golgi

被引：120

作者：

Fujita, Morihisa ^{[1
,5
]}

Maeda, Yusuke ^{[1
,2
]}

Ra, Moonjin ^{[3
]}

Yamaguchi, Yoshiki ^{[4
]}

Taguchi, Ryo ^{[3
,5
]}

Kinoshita, Taroh ^{[1
,2
,5
]}

机构：

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

[2] Osaka Univ, WPI Immunol Frontier Res Ctr, Suita, Osaka 5650871, Japan

[3] Univ Tokyo, Grad Sch Med, Tokyo 1130033, Japan

[4] RIKEN ASI, Struct Glycobiol Team, Saitama 3510198, Japan

[5] Japan Sci & Technol Agcy, Core Res Evolut Sci & Technol, Saitama 3320012, Japan

来源：

CELL | 2009年 / 139卷 / 02期

基金：

日本科学技术振兴机构;

关键词：

COPII-COATED VESICLES; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; MAMMALIAN-CELLS; INOSITOL DEACYLATION; RECYCLING PATHWAY; MDCK CELLS; GLYCOSYLPHOSPHATIDYLINOSITOL; YEAST; MEMBRANE;

D O I：

10.1016/j.cell.2009.08.040

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 proteins are attached to the cell surface via glycosylphosphatidylinositol (GPI) anchors. How GPI-anchored proteins (GPI-APs) are trafficked from the endoplasmic reticulum (ER) to the cell surface is poorly understood, but the GPI moiety has been postulated to function as a signal for sorting and transport. Here, we established mutant cells that were selectively defective in transport of GPI-APs from the ER to the Golgi. We identified a responsible gene, designated PGAP5 (post-GPI-attachment to proteins 5). PGAP5 belongs to a dimetal-containing phosphoesterase family and catalyzed the remodeling of the glycan moiety on GPI-APs. PGAP5 catalytic activity is a prerequisite for the efficient exit of GPI-APs from the ER. Our data demonstrate that GPI glycan acts as an ER-exit signal and suggest that glycan remodeling mediated by PGAP5 regulates GPI-AP transport in the early secretory pathway.

引用

页码：352 / 365

页数：14

共 48 条

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