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Actin-dependent α-catenin oligomerization contributes to adherens junction assembly

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  • Regina B. Troyanovsky

    (The Feinberg School of Medicine)

  • Indrajyoti Indra

    (The Feinberg School of Medicine)

  • Sergey M. Troyanovsky

    (The Feinberg School of Medicine
    The Feinberg School of Medicine)

Abstract

Classic cadherins, specifically E-cadherin in most epithelial cells, are transmembrane adhesion receptors, whose intracellular region interacts with proteins, termed catenins, forming the cadherin-catenin complex (CCC). The cadherin ectodomain generates 2D adhesive clusters (E-clusters) through cooperative trans and cis interactions, while catenins anchor the E-clusters to the actin cytoskeleton. How these two types of interactions are coordinated in the formation of specialized cell-cell adhesions, adherens junctions (AJ), remains unclear. Here, we focus on the role of the actin-binding domain of α-catenin (αABD) by showing that the interaction of the αABD with actin generates actin-bound linear CCC oligomers (CCC/actin strands) incorporating up to six CCCs. This actin-driven CCC oligomerization, which is cadherin ectodomain independent, preferentially occurs along the actin cortex enriched with key basolateral proteins, myosin-1c, scribble, and DLG1. In cell-cell contacts, the CCC/actin strands integrate with the E-clusters giving rise to the composite oligomers, E/actin clusters. Targeted inactivation of strand formation by point mutations emphasizes the importance of this oligomerization process for blocking intercellular protrusive membrane activity and for coupling AJs with the actomyosin-derived tensional forces.

Suggested Citation

  • Regina B. Troyanovsky & Indrajyoti Indra & Sergey M. Troyanovsky, 2025. "Actin-dependent α-catenin oligomerization contributes to adherens junction assembly," Nature Communications, Nature, vol. 16(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57079-z
    DOI: 10.1038/s41467-025-57079-z
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    References listed on IDEAS

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    1. Noboru Ishiyama & Ritu Sarpal & Megan N. Wood & Samantha K. Barrick & Tadateru Nishikawa & Hanako Hayashi & Anna B. Kobb & Annette S. Flozak & Alex Yemelyanov & Rodrigo Fernandez-Gonzalez & Shigenobu , 2018. "Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions," Nature Communications, Nature, vol. 9(1), pages 1-17, December.
    2. Yinghao Wu & Jeremie Vendome & Lawrence Shapiro & Avinoam Ben-Shaul & Barry Honig, 2011. "Transforming binding affinities from three dimensions to two with application to cadherin clustering," Nature, Nature, vol. 475(7357), pages 510-513, July.
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