Flotillin microdomains stabilize cadherins at cell-cell junctions

J Cell Sci. 2013 Nov 15;126(Pt 22):5293-304. doi: 10.1242/jcs.133975. Epub 2013 Sep 17.

Abstract

Cadherins are essential in many fundamental processes and assemble at regions of cell-cell contact in large macromolecular complexes named adherens junctions. We have identified flotillin 1 and 2 as new partners of the cadherin complexes. We show that flotillins are localised at cell-cell junctions (CCJs) in a cadherin-dependent manner. Flotillins and cadherins are constitutively associated at the plasma membrane and their colocalisation at CCJ increases with CCJ maturation. Using three-dimensional structured illumination super-resolution microscopy, we found that cadherin and flotillin complexes are associated with F-actin bundles at CCJs. The knockdown of flotillins dramatically affected N- and E-cadherin recruitment at CCJs in mesenchymal and epithelial cell types and perturbed CCJ integrity and functionality. Moreover, we determined that flotillins are required for cadherin association with GM1-containing plasma membrane microdomains. This allows p120 catenin binding to the cadherin complex and its stabilization at CCJs. Altogether, these data demonstrate that flotillin microdomains are required for cadherin stabilization at CCJs and for the formation of functional CCJs.

Keywords: Cadherins; Cell–cell junctions; Flotillins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Cadherins
  • Catenins
  • Membrane Proteins
  • Sphingolipid Activator Proteins
  • flotillins
  • Delta Catenin
  • CTNND1 protein, human