Spontaneous insertion and partitioning of alkaline phosphatase into model lipid rafts
Several cell surface eukaryotic proteins have a glycosylphosphatidylinositol (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...
Gespeichert in:
Veröffentlicht in: | EMBO reports 2002-05, Vol.3 (5), p.485-490 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | Several cell surface eukaryotic proteins have a glycosylphosphatidylinositol (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–dioleoylphosphatidylcholine 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. |
---|---|
ISSN: | 1469-221X 1469-3178 |
DOI: | 10.1093/embo-reports/kvf096 |