Thinking outside the cell: how cadherins drive adhesion

被引:252
作者
Brasch, Julia [1 ]
Harrison, Oliver J. [1 ,2 ]
Honig, Barry [1 ,2 ,3 ]
Shapiro, Lawrence [1 ]
机构
[1] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[2] Columbia Univ, Howard Hughes Med Inst, New York, NY 10032 USA
[3] Columbia Univ, Ctr Computat Biol & Bioinformat, New York, NY 10032 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
II CLASSIC CADHERINS; ADHERENS JUNCTIONS; STRUCTURAL BASIS; FUNCTIONAL-ANALYSIS; ALPHA-CATENIN; T-CADHERIN; BINDING; DOMAIN; SPECIFICITY; MECHANISM;
D O I
10.1016/j.tcb.2012.03.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cadherins are a superfamily of cell surface glycoproteins whose ectodomains contain multiple repeats of beta-sandwich extracellular cadherin (EC) 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 that drives junction assembly following cell cell contact by reducing the entropic cost associated with the formation of lateral cis oligomers. Cadherins outside the classical subfamily appear to have evolved distinct adhesive mechanisms that are only now beginning to be understood.
引用
收藏
页码:299 / 310
页数:12
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