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
Kenworthy AK
中科院分区:
生物学2区
文献类型:
--
作者:
Day CA;Kenworthy AK

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脂筏是细胞膜中脂质和蛋白质的假定复合物,被认为在运输和信号事件中起作用。CTxB(霍乱毒素B亚基)已成为筏相关蛋白研究最多的例子之一。由霍乱毒素的膜结合结构域组成,CTxB在宿主细胞的质膜上结合多达五个拷贝的其脂质受体。这种结合的多价性使毒素能够通过交联小的和瞬时的脂筏来重组下面的膜结构。因此,CTxB作为一个有用的模型,了解蛋白质稳定结构域的属性和功能。在本章中,我们总结了目前的证据表明,CTxB协会和交联脂筏,讨论如何CTxB结合调节膜结构域的架构和动态,并描述了这种交联行为的功能后果毒素摄取到细胞通过内吞作用。
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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