Spontaneous insertion and partitioning of alkaline phosphatase into model lipid rafts

被引:112
作者
Milhiet, PE
Giocondi, MC
Baghdadi, O
Ronzon, F
Roux, B
Le Grimellec, C
机构
[1] Univ Montpellier 1, CNRS, UMR 5048, Ctr Biochim Struct,INSERM,UMR554, F-34090 Montpellier, France
[2] Univ Paris 12, Lab CRRET, F-94000 Creteil, France
[3] Univ Lyon 1, CNRS, UMR 5013, Lab Physicochim Biol, F-69622 Villeurbanne, France
关键词
D O I
10.1093/embo-reports/kvf096
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
Several cell surface eukaryotic proteins have a glycosyl-phosphatidylinositol (GPI) modification at the C-terminal end that serves as an anchor to the plasma membrane and could be responsible for the presence of GPI proteins in rafts, a type of functionally important membrane microdomain enriched in sphingolipids and cholesterol. In order to understand better how GPI proteins partition into rafts, the insertion of the GPI-anchored alkaline phosphatase (AP) was studied in real-time using atomic force microscopy. Supported phospholipid bilayers made of a mixture of sphingomyelin-dioleoylphosphaticlylcholine containing cholesterol (Chl+) or not (Chl-) were used to mimic the fluid-ordered lipid phase separation in biological membranes. Spontaneous insertion of AP through its GPI anchor was observed inside both Chl+ and Chl- lipid ordered domains, but AP insertion was markedly increased by the presence of cholesterol.
引用
收藏
页码:485 / 490
页数:6
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