Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actin Cytoskeleton / metabolism*
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Actins / metabolism*
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Adherens Junctions / physiology*
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Animals
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Cell Adhesion / physiology
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Cells, Cultured
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Cytoskeletal Proteins / deficiency
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Epithelial Cells / metabolism*
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Epithelial Cells / ultrastructure
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Fetal Proteins / metabolism*
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Formins
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Keratinocytes
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Mice
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Microfilament Proteins
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Nuclear Proteins / metabolism*
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Polymers / metabolism
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Protein Binding / physiology
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Protein Structure, Tertiary / physiology
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Recombinant Fusion Proteins / metabolism
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Trans-Activators / metabolism
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alpha Catenin
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beta Catenin
Substances
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Actins
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CTNNB1 protein, mouse
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Ctnna1 protein, mouse
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Cytoskeletal Proteins
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Fetal Proteins
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Formins
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Microfilament Proteins
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Nuclear Proteins
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Polymers
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Recombinant Fusion Proteins
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Trans-Activators
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alpha Catenin
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beta Catenin