Afadin regulates actomyosin organization through αE-catenin at adherens junctions.
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Caderinas
/
Junções Aderentes
/
Beta Catenina
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Proteínas dos Microfilamentos
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article