Inter-cellular exchange of cellular components via VE-cadherin-dependent trans-endocytosis

PLoS One. 2014 Mar 6;9(6):e90736. doi: 10.1371/journal.pone.0090736. eCollection 2014.

Abstract

Cell-cell communications typically involve receptor-mediated signaling initiated by soluble or cell-bound ligands. Here, we report a unique mode of endocytosis: proteins originating from cell-cell junctions and cytosolic cellular components from the neighboring cell are internalized, leading to direct exchange of cellular components between two adjacent endothelial cells. VE-cadherins form transcellular bridges between two endothelial cells that are the basis of adherence junctions. At such adherens junction sites, we observed the movement of the entire VE-cadherin molecule from one endothelial cell into the other with junctional and cytoplasmic components. This phenomenon, here termed trans-endocytosis, requires the establishment of a VE-cadherin homodimer in trans with internalization proceeding in a Rac1-, and actomyosin-dependent manner. Importantly, the trans-endocytosis is not dependent on any known endocytic pathway including clathrin-dependent endocytosis, macropinocytosis or phagocytosis. This novel form of cell-cell communications, leading to a direct exchange of cellular components, was observed in 2D and 3D-cultured endothelial cells as well as in the developing zebrafish vasculature.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Antigens, CD / metabolism*
  • COS Cells
  • Cadherins / metabolism*
  • Cell Communication
  • Chlorocebus aethiops
  • Coculture Techniques
  • Endocytosis*
  • Human Umbilical Vein Endothelial Cells / metabolism*
  • Humans
  • Myosins / metabolism
  • Protein Transport
  • Vinculin / metabolism
  • Zebrafish
  • rac1 GTP-Binding Protein / metabolism

Substances

  • Actins
  • Antigens, CD
  • Cadherins
  • cadherin 5
  • Vinculin
  • Myosins
  • rac1 GTP-Binding Protein