Article abstract
Nature Cell Biology 6, 21 - 30 (2003)
Published online: 30 November 2003 | doi:10.1038/ncb1075
Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
Agnieszka Kobielak1, H. Amalia Pasolli1 & Elaine Fuchs1
Abstract
During epithelial sheet formation, linear actin cables assemble at nascent adherens junctions. This process requires 
-catenin and actin polymerization, although the underlying mechanism is poorly understood. Here, we show that formin-1 interacts with -catenin, localizes to adherens junctions and nucleates unbranched actin filaments. Furthermore, disruption of the -catenin–formin-1 interaction blocks assembly of radial actin cables and perturbs intercellular adhesion. A fusion protein of the 
-catenin-binding domain of -catenin with the actin polymerization domains of formin-1 rescues formation of adherens junctions and associated actin cables in -catenin-null keratinocytes. These findings provide new insight into how -catenin orchestrates actin dynamics during intercellular junction formation.
- Howard Hughes Medical Institute, Laboratory of Mammalian Cell Biology and Development, The Rockefeller University, 1230 York Avenue, Box 300, New York, NY 10021-6399, USA.
Correspondence to: Elaine Fuchs1 e-mail: fuchslb@rockefeller.edu
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