Related Experiment Video
Updated: Aug 22, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Published on: November 11, 2018
GPI-anchored protein cleavage in the regulation of transmembrane signals
Frances J Sharom1, Galina Radeva
1Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario, N1G 2W1 Canada.
Abstract:
The structure of covalently-linked glycosylphosphatidylinositol (GPI) anchors of membrane proteins displayed on the cell surface is described. Evidence of how the GPI-anchors are sorted into membrane rafts in the plasma membrane is reviewed. Proteins are released by hydrolysis of the linkage to the GPI anchor and phospholipases from different sources involved in this process are characterised. The regulation of protein conformation and function resulting from phospholipase cleavage of the GPI anchor is discussed in the context of its role in signal transduction by insulin. In this signalling system, re-distribution of critical membrane components, including GPI-anchored proteins and non-receptor tyrosine kinases, between different raft domains appears to play a central role in the signal transduction pathway.
Related Concept Videos
GPI Anchoring of Proteins in the ER Membrane
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Amplifying Signals via Enzymatic Cascade
IP3/DAG Signaling Pathway
GTPases and their Regulation
Large G-proteins, also known...
GTPases and their Regulation
Large G-proteins, also known...
Activation and Inactivation of G Proteins

