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

Verma, Suzie, Han, Siew Ping, Michael, Magdalene, Gomez, Guillermo, Yang, Zhe, Teasdale, Rohan D., Ratheesh, Aparna, Kovacs, Eva M., Ali, Radiya G. and Yap, Alpha S.K. (2012) A WAVE2-Arp2/3 actin nucleator apparatus supports junctional tension at the epithelial zonula adherens. Molecular Biology of The Cell, 23 23: 4601-4610. doi:10.1091/mbc.E12-08-0574

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Author Verma, Suzie
Han, Siew Ping
Michael, Magdalene
Gomez, Guillermo
Yang, Zhe
Teasdale, Rohan D.
Ratheesh, Aparna
Kovacs, Eva M.
Ali, Radiya G.
Yap, Alpha S.K.
Title A WAVE2-Arp2/3 actin nucleator apparatus supports junctional tension at the epithelial zonula adherens
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2012-12
Sub-type Article (original research)
DOI 10.1091/mbc.E12-08-0574
Open Access Status File (Publisher version)
Volume 23
Issue 23
Start page 4601
End page 4610
Total pages 10
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Collection year 2013
Language eng
Abstract 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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 14 Dec 2012, 10:57:52 EST by Susan Allen on behalf of Institute for Molecular Bioscience