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

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...

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Bibliographic Details
Published in:The Journal of cell biology 2016-04, Vol.213 (2), p.243-260
Main Authors: Choi, Wangsun, Acharya, Bipul R, Peyret, Grégoire, Fardin, Marc-Antoine, Mège, René-Marc, Ladoux, Benoit, Yap, Alpha S, Fanning, Alan S, Peifer, Mark
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - metabolism
Adherens Junctions - metabolism
Animals
Cell Adhesion
Cell adhesion & migration
Cell Shape
Cellular Biology
Cytoskeleton
Cytoskeleton - metabolism
Dogs
Epithelial Cells - metabolism
Epithelial Cells - ultrastructure
Gene Knockdown Techniques
Life Sciences
Madin Darby Canine Kidney Cells
Microfilament Proteins - metabolism
Microfilament Proteins - physiology
Morphogenesis
Proteins
Tissues
Zonula Occludens Proteins - genetics
Zonula Occludens Proteins - metabolism
Zonula Occludens Proteins - physiology
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201506115