Functions of cholera toxin B-subunit as a raft cross-linker.
Functions of cholera toxin B-subunit as a raft cross-linker.
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DOI:
10.1042/bse0570135
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发表时间:
2015
影响因子:
6.4
通讯作者:
Kenworthy AK
中科院分区:
文献类型:
--
作者:
Day CA;Kenworthy AK
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 cross-linking behaviour on toxin uptake into cells via endocytosis.
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