CELL SIGNALING BY GLYCOSYL-PHOSPHATIDYLIN OSITOL ANCHORED PROTEINS

Authors
Citation
F. Nazih et C. Delbart, CELL SIGNALING BY GLYCOSYL-PHOSPHATIDYLIN OSITOL ANCHORED PROTEINS, MS. Medecine sciences, 14(3), 1998, pp. 275-282
Citations number
37
Categorie Soggetti
Medicine, Research & Experimental
Journal title
ISSN journal
07670974
Volume
14
Issue
3
Year of publication
1998
Pages
275 - 282
Database
ISI
SICI code
0767-0974(1998)14:3<275:CSBGOA>2.0.ZU;2-8
Abstract
Recently a novel mechanism has been described for the hydrophobic atta chment of proteins to membranes which is shared by membrane proteins o f widely differing origins and functions. The hydrophobic anchor is a glycosyl-phosphatidylinositol (GPI) which is covalently attached to th e polypeptide chain. GPI-anchored proteins have been reported to resid e in clusters collected over small membrane invaginations called caveo lae. GPI-anchored proteins constitute an exceptionally diverse family of membrane molecules functioning in such processes as nutrient uptake , cell adhesion, catalysis, and membrane signalling events. A growing body of biochemical evidence indicates that they play a key role in th e recently discovered potocytosis process, act as intracellular sortin g signals, cause activation of Src-family kinase-mediated signalling p athways. Their hydrolysis, yielding inositolphosphoglycans and diacylg lycerol, is one of the earliest intracellular events generated in resp onse to growth factors, insulin or lipoproteins.