Afadin regulates actomyosin organization through αE-catenin at adherens junctions.

Shotaro Sakakibara, Kiyohito Mizutani, Ayumu Sugiura, Ayuko Sakane, Takuya Sasaki, Shigenobu Yonemura, Yoshimi Takai

The Journal of cell biology 2020 May 04

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Actomyosin-undercoated adherens junctions are critical for epithelial cell integrity and remodeling. Actomyosin associates with adherens junctions through αE-catenin complexed with β-catenin and E-cadherin in vivo; however, in vitro biochemical studies in solution showed that αE-catenin complexed with β-catenin binds to F-actin less efficiently than αE-catenin that is not complexed with β-catenin. Although a "catch-bond model" partly explains this inconsistency, the mechanism for this inconsistency between the in vivo and in vitro results remains elusive. We herein demonstrate that afadin binds to αE-catenin complexed with β-catenin and enhances its F-actin-binding activity in a novel mechanism, eventually inducing the proper actomyosin organization through αE-catenin complexed with β-catenin and E-cadherin at adherens junctions. © 2020 Sakakibara et al.

Citation

Shotaro Sakakibara, Kiyohito Mizutani, Ayumu Sugiura, Ayuko Sakane, Takuya Sasaki, Shigenobu Yonemura, Yoshimi Takai. Afadin regulates actomyosin organization through αE-catenin at adherens junctions. The Journal of cell biology. 2020 May 04;219(5)