Cadherins are transmembrane adhesion molecules that mediate homotypic cell–cell contact. In adherens junctions, the cytoplasmic domain of cadherins is functionally linked to the actin cytoskeleton through a series of proteins known as catenins. E-cadherin binds to β-catenin, which in turn binds to α-catenin to form a ternary complex. α-Catenin also binds to actin, and it was assumed previously that α-catenin links the cadherin–catenin complex to actin. However, biochemical, structural and live-cell imaging studies of the cadherin–catenin complex and its interaction with actin show that binding of β-catenin to α-catenin prevents the latter from binding to actin. Biochemical and structural data indicate that α-catenin acts as an allosteric protein whose conformation and activity changes depending on whether or not it is bound to β-catenin. Initial contacts between cells occur on dynamic lamellipodia formed by polymerization of branched actin networks, a process controlled by the Arp2/3 (actin-related protein 2/3) complex. α-Catenin can suppress the activity of Arp2/3 by competing for actin filaments. These findings lead to a model for adherens junction formation in which clustering of the cadherin–β-catenin complex recruits high levels of α-catenin that can suppress the Arp2/3 complex, leading to cessation of lamellipodial movement and formation of a stable contact. Thus α-catenin appears to play a central role in cell–cell contact formation.
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April 2008
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Conference Article|
March 20 2008
Biochemical and structural analysis of α-catenin in cell–cell contacts
Sabine Pokutta;
Sabine Pokutta
*Department of Structural Biology, D100 Fairchild Science Building, Stanford University School of Medicine, Stanford, CA 94305-5126, U.S.A.
†Department of Molecular and Cellular Physiology, Room B100, Beckman Center, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305-5345, U.S.A.
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Frauke Drees;
Frauke Drees
†Department of Molecular and Cellular Physiology, Room B100, Beckman Center, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305-5345, U.S.A.
‡Department of Biological Sciences, Gilbert Hall, Stanford University, Stanford, CA 94305-5020, U.S.A.
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Soichiro Yamada;
Soichiro Yamada
†Department of Molecular and Cellular Physiology, Room B100, Beckman Center, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305-5345, U.S.A.
‡Department of Biological Sciences, Gilbert Hall, Stanford University, Stanford, CA 94305-5020, U.S.A.
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W. James Nelson;
W. James Nelson
†Department of Molecular and Cellular Physiology, Room B100, Beckman Center, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305-5345, U.S.A.
‡Department of Biological Sciences, Gilbert Hall, Stanford University, Stanford, CA 94305-5020, U.S.A.
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William I. Weis
William I. Weis
1
*Department of Structural Biology, D100 Fairchild Science Building, Stanford University School of Medicine, Stanford, CA 94305-5126, U.S.A.
†Department of Molecular and Cellular Physiology, Room B100, Beckman Center, Stanford University School of Medicine, 279 Campus Drive, Stanford, CA 94305-5345, U.S.A.
1To whom correspondence should be addressed (email bill.weis@stanford.edu).
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Biochem Soc Trans (2008) 36 (2): 141–147.
Article history
Received:
January 01 2008
Citation
Sabine Pokutta, Frauke Drees, Soichiro Yamada, W. James Nelson, William I. Weis; Biochemical and structural analysis of α-catenin in cell–cell contacts. Biochem Soc Trans 1 April 2008; 36 (2): 141–147. doi: https://doi.org/10.1042/BST0360141
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