Rho GEFs in endothelial junctions effector selectivity and signaling integration determine junctional response

Research output: Contribution to journalComment/debate

5 Scopus citations

Abstract

Rho GTPases are cytoskeleton-regulating proteins that mediate the formation of intercellular junctions. Their localized activation by Rho GEFs (guanine-nucleotide exchange factors) and the selective activation of downstream effectors have emerged as areas of active research in the cell adhesion field. We reported recently that the Rho-specific GEFs Syx (Synectin-binding RhoA exchange factor) and TEM4 (Tumor Endothelial Marker 4) are both essential for endothelial junction maturation and barrier function. Syx is recruited to cell contacts via its C-terminal PDZ binding motif and it's interaction with Mupp1 and the Crumbs polarity complex, while the junctional localization of TEM4 requires it's N-terminal domain and interaction with the cadherin-catenin complex. Our findings support multiple roles for RhoA in junction formation and maintenance. They also suggest that selective coupling of RhoA activation to Dia1 and/or ROCK signaling is critical for determining endothelial junction integrity.

Original languageEnglish (US)
JournalTissue Barriers
Volume1
Issue number5
StatePublished - Dec 2013

Keywords

  • Adhesion
  • Cadherin
  • Cell junctions
  • Endothelial
  • Epithelial
  • GEFs
  • References
  • Rho GTPases

ASJC Scopus subject areas

  • Biochemistry
  • Histology
  • Cell Biology

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