Lipid rafts are putative complexes of lipids and proteins in cellular membranes that are proposed to function in trafficking and signalling events. CTxB (cholera toxin B-subunit) has emerged as one of the most studied examples of a raft-associated protein. Consisting of the membrane-binding domain of cholera toxin, CTxB binds up to five copies of its lipid receptor on the plasma membrane of the host cell. This multivalency of binding gives the toxin the ability to reorganize underlying membrane structure by cross-linking otherwise small and transient lipid rafts. CTxB thus serves as a useful model for understanding the properties and functions of protein-stabilized domains. In the present chapter, we summarize current evidence that CTxB associates with and cross-links lipid rafts, discuss how CTxB binding modulates the architecture and dynamics of membrane domains, and describe the functional consequences of this crosslinking behaviour on toxin uptake into cells via endocytosis.
|Original language||English (US)|
|Number of pages||11|
|Journal||Essays in Biochemistry|
|State||Published - 2015|
Bibliographical notePublisher Copyright:
© The Authors Journal compilation © 2015 Biochemical Society.
- Cholera toxin
- Giant plasma membrane vesicle
- Lipid raft
- Membrane curvature
- Membrane domain