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

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.
Mesh Terms:
Actins, Adherens Junctions, Animals, Cell Adhesion, Cells, Cultured, Cytoskeletal Proteins, Epithelial Cells, Fetal Proteins, Keratinocytes, Mice, Microfilament Proteins, Microfilaments, Nuclear Proteins, Polymers, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Trans-Activators, alpha Catenin, beta Catenin
Nat. Cell Biol.
Date: Jan. 01, 2004
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