Dimer asymmetry defines α-catenin interactions.
Dimer asymmetry defines α-catenin interactions.
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DOI：
10.1038/nsmb.2479
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发表时间：
2013-02
影响因子：
16.8
通讯作者：
Izard, Tina
中科院分区：
文献类型：
--
作者：
Rangarajan, Erumbi S.;Izard, Tina
The F-actin binding cytoskeletal protein α-catenin interacts with β-catenin-cadherin complexes and stabilizes cell-cell junctions. The β-catenin–α-catenin complex cannot bind to F-actin, whereas interactions of α-catenin with the cytoskeletal protein vinculin appear necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human α-catenin at 3.7 Å resolution. α-Catenin forms an asymmetric dimer, where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, where the two subunits have remarkably different conformations. The crystal structure explains why dimeric α-catenin has a higher affinity for F-actin than monomeric α-catenin, why the β-catenin–α-catenin complex does not bind to F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton, and why α-catenin but not inactive vinculin can bind to F-actin.
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