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Afadin regulates actomyosin organization through αE-catenin at adherens junctions.
Sakakibara, Shotaro; Mizutani, Kiyohito; Sugiura, Ayumu; Sakane, Ayuko; Sasaki, Takuya; Yonemura, Shigenobu; Takai, Yoshimi.
Afiliação
  • Sakakibara S; Division of Pathogenetic Signaling, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
  • Mizutani K; Department of Biochemistry, Tokushima University Graduate School of Medical Sciences, Tokushima, Japan.
  • Sugiura A; Division of Pathogenetic Signaling, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
  • Sakane A; Division of Pathogenetic Signaling, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
  • Sasaki T; Department of Biochemistry, Tokushima University Graduate School of Medical Sciences, Tokushima, Japan.
  • Yonemura S; Department of Interdisciplinary Researches for Medicine and Photonics, Institute of Post-LED Photonics, Tokushima University, Tokushima, Japan.
  • Takai Y; Department of Biochemistry, Tokushima University Graduate School of Medical Sciences, Tokushima, Japan.
J Cell Biol ; 219(5)2020 05 04.
Article em En | MEDLINE | ID: mdl-32227204
ABSTRACT
Actomyosin-undercoated adherens junctions are critical for epithelial cell integrity and remodeling. Actomyosin associates with adherens junctions through αE-catenin complexed with ß-catenin and E-cadherin in vivo; however, in vitro biochemical studies in solution showed that αE-catenin complexed with ß-catenin binds to F-actin less efficiently than αE-catenin that is not complexed with ß-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 ß-catenin and enhances its F-actin-binding activity in a novel mechanism, eventually inducing the proper actomyosin organization through αE-catenin complexed with ß-catenin and E-cadherin at adherens junctions.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Caderinas / Junções Aderentes / Beta Catenina / Proteínas dos Microfilamentos Limite: Animals / Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Caderinas / Junções Aderentes / Beta Catenina / Proteínas dos Microfilamentos Limite: Animals / Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article