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J Cell Biol. 2016 Apr 25;213(2):243-60. doi: 10.1083/jcb.201506115.

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

Author information

1
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 peifer@unc.edu fanningalan@gmail.com wchoi@email.unc.edu.
2
Division of Cell Biology and Molecular Medicine, Institute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland, Australia 4072.
3
Institut Jacques Monod, Centre National de la Recherche Scientifique UMR 7592 and Université Paris Diderot, 75013 Paris, France.
4
Institut Jacques Monod, Centre National de la Recherche Scientifique UMR 7592 and Université Paris Diderot, 75013 Paris, France Mechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
5
Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 Department of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
6
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 peifer@unc.edu fanningalan@gmail.com wchoi@email.unc.edu.

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.

Comment in

PMID:
27114502
PMCID:
PMC5084271
DOI:
10.1083/jcb.201506115
[Indexed for MEDLINE]
Free PMC Article

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