Protein Association with Membrane Rafts
Published Online: 15 JUN 2011
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Veit, M. and Thaa, B. 2011. Protein Association with Membrane Rafts. eLS. .
- Published Online: 15 JUN 2011
Membrane rafts are very small and highly dynamic assemblies in cellular membranes enriched in cholesterol and sphingolipids. Some proteins can functionally associate with rafts: peripheral membrane proteins are incorporated into rafts depending on cues such as the presence of a glycosyl-phosphatidylinositol (GPI) anchor or S-acylation (palmitoylation); transmembrane proteins can partition into raft domains depending on specific features within their transmembrane domain. Raft association of membrane proteins was originally defined by their resistance to cold Triton X-100 extraction, which is however insufficient as the sole criterion – more sophisticated methodology such as fluorescence resonance energy transfer (FRET) has to be employed to determine whether and how a given protein interacts with raft structures.
Membrane rafts are small, dynamic clusters within biological membranes enriched in cholesterol and sphingolipids.
Rafts can be coalesced and stabilised to fulfil a biological function, for example, signal transduction or virus budding.
Some proteins are capable of partitioning into raft domains.
Raft-targeting features in proteins are glycosyl-phosphatidylinositol (GPI) anchors, S-acylation (palmitoylation) and structural motifs in the transmembrane domain.
Assessment of detergent-resistant membranes (DRM), the original biochemical method to analyse raft association of a protein, is artefact-prone and therefore not suitable to prove raft involvement in a biological process.
More sophisticated methodology such as fluorescence resonance energy transfer (FRET) is needed to decipher raft association of a protein.
- membrane raft;
- glycosyl-phosphatidylinositol (GPI) anchor;
- detergent-resistant membranes (DRM);
- fluorescence microscopy;
- fluorescence resonance energy transfer (FRET);
- model membranes