Thinking outside the cell: how cadherins drive adhesion.
Thinking outside the cell: how cadherins drive adhesion.
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DOI：
10.1016/j.tcb.2012.03.004
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发表时间：
2012-06
影响因子：
19
通讯作者：
Shapiro L
中科院分区：
文献类型：
--
作者：
Brasch J;Harrison OJ;Honig B;Shapiro L
钙粘蛋白体现细胞表面糖蛋白的超家族，其胞外域含有β-夹心EC（胞外钙粘蛋白）结构域的多个重复，其采用与免疫球蛋白结构域类似的折叠。最具特征的钙粘蛋白是脊椎动物“经典”钙粘蛋白，其通过从贴壁细胞延伸的膜远端EC 1结构域之间的反式同源二聚化介导粘附，并通过顺式聚集组装细胞间粘附连接。为了形成成熟的反式粘附二聚体，来自贴壁细胞的钙粘蛋白结构域以“链交换”构象二聚化。这发生在两步结合过程中，涉及称为“X-二聚体”的快速结合中间体。反式二聚体比钙粘蛋白单体柔性低，这是通过降低与横向顺式寡聚体形成相关的熵成本来驱动细胞-细胞接触后的连接组装的因素。钙粘蛋白以外的经典亚家族似乎已经演变出独特的粘附机制，这是刚刚开始被理解。
Cadherins embody a superfamily of cell-surface glycoproteins whose ectodomains contain multiple repeats of β-sandwich EC (extracellular cadherin) domains that adopt a similar fold to immunoglobulin domains. The best characterized cadherins are the vertebrate “classical” cadherins, which mediate adhesion via trans homodimerization between their membrane-distal EC1 domains that extend from apposed cells, and assemble intercellular adherens junctions through cis clustering. To form mature trans adhesive dimers, cadherin domains from apposed cells dimerize in a “strand-swapped” conformation. This occurs in a two-step binding process involving a fast-binding intermediate called the “X-dimer”. Trans dimers are less flexible than cadherin monomers, a factor which drives junction assembly following cell-cell contact by reducing the entropic cost associated with the formation of lateral cis oligomers. Cadherins outside of the classical subfamily appear to have evolved distinct adhesive mechanisms which are just now beginning to be understood.
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影响因子：
7.5
作者：
Harris ES;Nelson WJ
通讯作者：
Nelson WJ
DOI：
10.1073/pnas.1006284107
发表时间：
2010-06-08
影响因子：
11.1
作者：
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通讯作者：
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影响因子：
4
作者：
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通讯作者：
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影响因子：
3.4
作者：
Bayas, MV;Leung, A;Leckband, D
通讯作者：
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影响因子：
5.6
作者：
Brasch J;Harrison OJ;Ahlsen G;Carnally SM;Henderson RM;Honig B;Shapiro L
通讯作者：
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