Cortactin scaffolds Arp2/3 and WAVE2 at the epithelial zonula adherens.
J Biol Chem
; 289(11): 7764-75, 2014 Mar 14.
Article
en En
| MEDLINE
| ID: mdl-24469447
ABSTRACT
Cadherin junctions arise from the integrated action of cell adhesion, signaling, and the cytoskeleton. At the zonula adherens (ZA), a WAVE2-Arp2/3 actin nucleation apparatus is necessary for junctional tension and integrity. But how this is coordinated with cadherin adhesion is not known. We now identify cortactin as a key scaffold for actin regulation at the ZA, which localizes to the ZA through influences from both E-cadherin and N-WASP. Using cell-free protein expression and fluorescent single molecule coincidence assays, we demonstrate that cortactin binds directly to the cadherin cytoplasmic tail. However, its concentration with cadherin at the apical ZA also requires N-WASP. Cortactin is known to bind Arp2/3 directly (Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A., and Parsons, J. T. (2000) J. Cell Biol. 151, 29-40). We further show that cortactin can directly bind WAVE2, as well as Arp2/3, and both these interactions are necessary for actin assembly at the ZA. We propose that cortactin serves as a platform that integrates regulators of junctional actin assembly at the ZA.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Uniones Adherentes
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Epitelio
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Proteína 2 Relacionada con la Actina
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Proteína 3 Relacionada con la Actina
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Cortactina
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Familia de Proteínas del Síndrome de Wiskott-Aldrich
Límite:
Humans
Idioma:
En
Revista:
J Biol Chem
Año:
2014
Tipo del documento:
Article
País de afiliación:
Australia