A WAVE2-Arp2/3 actin nucleator apparatus supports junctional tension at the epithelial zonula adherens

The epithelial zonula adherens (ZA) is a specialized adhesive junction where actin dynamics and myosin-driven contractility coincide. The junctional cytoskeleton is enriched in myosin II, which generates contractile force to support junctional tension. It is also enriched in dynamic actin filaments,...

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Bibliographic Details
Published in:Molecular biology of the cell 2012-12, Vol.23 (23), p.4601-4610
Main Authors: Verma, Suzie, Han, Siew Ping, Michael, Magdalene, Gomez, Guillermo A, Yang, Zhe, Teasdale, Rohan D, Ratheesh, Aparna, Kovacs, Eva M, Ali, Radiya G, Yap, Alpha S
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - metabolism
Actin Cytoskeleton - ultrastructure
Actin-Related Protein 2 - metabolism
Actin-Related Protein 2-3 Complex - metabolism
Actin-Related Protein 2-3 Complex - ultrastructure
Actin-Related Protein 3 - metabolism
Actins - metabolism
Actins - ultrastructure
Adherens Junctions - metabolism
Adherens Junctions - ultrastructure
Caco-2 Cells
Epithelium - metabolism
Humans
Nonmuscle Myosin Type IIA - metabolism
Nonmuscle Myosin Type IIB - metabolism
Signal Transduction
Wiskott-Aldrich Syndrome Protein Family - metabolism
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Summary:The epithelial zonula adherens (ZA) is a specialized adhesive junction where actin dynamics and myosin-driven contractility coincide. The junctional cytoskeleton is enriched in myosin II, which generates contractile force to support junctional tension. It is also enriched in dynamic actin filaments, which are replenished by ongoing actin assembly. In this study we sought to pursue the relationship between actin assembly and junctional contractility. We demonstrate that WAVE2-Arp2/3 is a major nucleator of actin assembly at the ZA and likely acts in response to junctional Rac signaling. Furthermore, WAVE2-Arp2/3 is necessary for junctional integrity and contractile tension at the ZA. Maneuvers that disrupt the function of either WAVE2 or Arp2/3 reduced junctional tension and compromised the ability of cells to buffer side-to-side forces acting on the ZA. WAVE2-Arp2/3 disruption depleted junctions of both myosin IIA and IIB, suggesting that dynamic actin assembly may support junctional tension by facilitating the local recruitment of myosin.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.e12-08-0574