Powered by OpenAIRE graph
image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Journal of Cell Scie...arrow_drop_down
image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
Journal of Cell Science
Article . 2013 . Peer-reviewed
Data sources: Crossref
versions View all 2 versions

Flotillin micro-domains stabilize Cadherins at cell-cell junctions

Authors: Nam Do Khoa; Cécile Gauthier-Rouvière; Franck Comunale; Stéphane Bodin; Emilie Guillaume; Damien Planchon;

Flotillin micro-domains stabilize Cadherins at cell-cell junctions

Abstract

Cadherins are essential in many fundamental processes and assemble at regions of cell-cell contact in large macromolecular complexes named adherens junctions. Here, we identified Flotillin 1 and 2 as new partners of the Cadherin complexes. We show that Flotillins are localized at cell-cell junctions (CCJ) in a Cadherin-dependent manner. Flotillins and Cadherins are constitutively associated at the plasma membrane and their colocalization at CCJ increases with CCJ maturation. Using 3D-SIM super-resolution microscopy, we demonstrate that Cadherins and Flotillins complexes are associated with F-actin bundles at CCJ. The knockdown of Flotillins dramatically affected N- and E-cadherin recruitment at CCJ in mesenchymal and epithelial cell types and perturbed CCJ integrity and functionality. Moreover, we show that Flotillins are required for Cadherin association with GM1-containing plasma membrane micro-domains. This allows p120 Catenin binding to the Cadherin complex and its stabilization at CCJ. Altogether, these data demonstrate that Flotillin micro-domains are required for Cadherin stabilization at CCJ and for the formation of functional CCJ.

Keywords

Sphingolipid Activator Proteins, Delta Catenin, Cell Membrane, Membrane Proteins, Catenins, Cadherins, HCT116 Cells, Protein Structure, Tertiary, Intercellular Junctions, Gene Knockdown Techniques, MCF-7 Cells, Humans

  • BIP!
    Impact byBIP!
    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    48
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 10%
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Top 10%
Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
48
Top 10%
Top 10%
Top 10%
bronze