Remodeling the zonula adherens in response to tension and the role of afadin in this response

Choi, Wangsun, Acharya, Bipul R., Peyret, Grégoire, Fardin, Marc-Antoine, Mège, René-Marc, Ladoux, Benoit, Yap, Alpha S., Fanning, Alan S. and Peifer, Mark (2016) Remodeling the zonula adherens in response to tension and the role of afadin in this response. Journal of Cell Biology, 213 2: 243-260. doi:10.1083/jcb.201506115


Author Choi, Wangsun
Acharya, Bipul R.
Peyret, Grégoire
Fardin, Marc-Antoine
Mège, René-Marc
Ladoux, Benoit
Yap, Alpha S.
Fanning, Alan S.
Peifer, Mark
Title Remodeling the zonula adherens in response to tension and the role of afadin in this response
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 1540-8140
0021-9525
Publication date 2016-04-25
Year available 2016
Sub-type Article (original research)
DOI 10.1083/jcb.201506115
Open Access Status DOI
Volume 213
Issue 2
Start page 243
End page 260
Total pages 18
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Language eng
Abstract Morphogenesis requires dynamic coordination between cell-cell adhesion and the cytoskeleton to allow cells to change shape and move without losing tissue integrity. We used genetic tools and superresolution microscopy in a simple model epithelial cell line to define how the molecular architecture of cell-cell zonula adherens (ZA) is modified in response to elevated contractility, and how these cells maintain tissue integrity. We previously found that depleting zonula occludens 1 (ZO-1) family proteins in MDCK cells induces a highly organized contractile actomyosin array at the ZA. We find that ZO knockdown elevates contractility via a Shroom3/Rho-associated, coiled-coil containing protein kinase (ROCK) pathway. Our data suggest that each bicellular border is an independent contractile unit, with actin cables anchored end-on to cadherin complexes at tricellular junctions. Cells respond to elevated contractility by increasing junctional afadin. Although ZO/afadin knockdown did not prevent contractile array assembly, it dramatically altered cell shape and barrier function in response to elevated contractility. We propose that afadin acts as a robust protein scaffold that maintains ZA architecture at tricellular junctions
Keyword Morphogenesis
Afadin
Zonula adherens
Cell-cell adhesion
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID R01GM47957
617233
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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