Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables

被引：296

作者：

Kobielak, A ^{[1
]}

Pasolli, HA ^{[1
]}

Fuchs, E ^{[1
]}

机构：

[1] Rockefeller Univ, Howard Hughes Med Inst, Lab Mammalian Cell Biol & Dev, New York, NY 10021 USA

来源：

NATURE CELL BIOLOGY | 2004年 / 6卷 / 01期

关键词：

D O I：

10.1038/ncb1075

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

During epithelial sheet formation, linear actin cables assemble at nascent adherens junctions. This process requires alpha-catenin and actin polymerization, although the underlying mechanism is poorly understood. Here, we show that formin-1 interacts with alpha-catenin, localizes to adherens junctions and nucleates unbranched actin filaments. Furthermore, disruption of the alpha-catenin-formin-1 interaction blocks assembly of radial actin cables and perturbs intercellular adhesion. A fusion protein of the beta-catenin-binding domain of alpha-catenin with the actin polymerization domains of formin-1 rescues formation of adherens junctions and associated actin cables in alpha-catenin-null keratinocytes. These findings provide new insight into how alpha-catenin orchestrates actin dynamics during intercellular junction formation.

引用

页码：21 / U2

页数：11

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