Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: Recent progress

被引：216

作者：

Kinoshita, Taroh ^{[1
,2
,3
]}

Fujita, Morihisa ^{[2
,3
]}

Maeda, Yusuke ^{[1
,2
,4
]}

机构：

[1] Osaka Univ, WPI Immunol Frontier Res Ctr, Osaka, Japan

[2] Osaka Univ, Res Inst Microbial Dis, Osaka, Japan

[3] CREST, Saitama, Japan

[4] Japan Soc Technol, PREST, Saitama, Japan

来源：

JOURNAL OF BIOCHEMISTRY | 2008年 / 144卷 / 03期

关键词：

endoplasmic reticulum; fatty acid; glycosyltransferases; Golgi apparatus; post-translational modification;

D O I：

10.1093/jb/mvn090

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：

More than 100 mammalian proteins are post-translationally modified by glycosylphosphatidylinositol (GPI) at their C-termini and are anchored to the cell surface membrane via the lipid portion. GPI-anchored proteins (GPI-APs) have various functions, such as hydrolytic enzymes, receptors, adhesion molecules, complement regulatory proteins and other immunologically important proteins. GPI-anchored proteins are mainly associated with membrane microdomains or membrane rafts enriched in sphingolipids and cholesterol. It is thought that association with membrane rafts is important for GPI-APs in signal transduction and other functions. Here, we review recent progress in studies on biosynthesis, remodelling and functions of mammalian GPI-APs.

引用

页码：287 / 294

页数：8

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