Monomeric α-catenin links cadherin to the actin cytoskeleton

被引：148

作者：

Desai, Ridhdhi ^{[1
]}

Sarpal, Ritu ^{[1
]}

Ishiyama, Noboru ^{[2
,3
]}

Pellikka, Milena ^{[1
]}

Ikura, Mitsuhiko ^{[2
,3
]}

Tepass, Ulrich ^{[1
]}

机构：

[1] Univ Toronto, Dept Cell & Syst Biol, Toronto, ON M5S 3G5, Canada

[2] Univ Toronto, Ontario Canc Inst, Toronto, ON M5G 1L7, Canada

[3] Univ Toronto, Dept Med Biophys, Toronto, ON M5G 1L7, Canada

来源：

NATURE CELL BIOLOGY | 2013年 / 15卷 / 03期

关键词：

MEDIATED CELL-ADHESION; ADHERENS JUNCTIONS; BETA-CATENIN; DE-CADHERIN; F-ACTIN; IN-VITRO; DROSOPHILA; COMPLEX; MORPHOGENESIS; VINCULIN;

D O I：

10.1038/ncb2685

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The linkage of adherens junctions to the actin cytoskeleton is essential for cell adhesion. The contribution of the cadherin-catenin complex to the interaction between actin and the adherens junction remains an intensely investigated subject that centres on the function of alpha-catenin, which binds to cadherin through beta-catenin and can bind F-actin directly or indirectly. Here, we delineate regions within Drosophila alpha-Catenin (alpha-Cat) that are important for adherens junction performance in static epithelia and dynamic morphogenetic processes. Moreover, we address whether persistent alpha-catenin-mediated physical linkage between cadherin and F-actin is crucial for cell adhesion and characterize the functions of alpha-catenin monomers and dimers at adherens junctions. Our data support the view that monomeric alpha-catenin acts as an essential physical linker between the cadherin beta-catenin complex and the actin cytoskeleton, whereas alpha-catenin dimers are cytoplasmic and form an equilibrium with monomeric junctional alpha-catenin.

引用

页码：261 / 273

页数：13

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