VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation

Benjamin F. Brinkmann, Tim Steinbacher, Christian Hartmann, Daniel Kummer, Denise Pajonczyk, Fatemeh Mirzapourshafyi, Masanori Nakayama, Thomas Weide, Volker Gerke, Klaus Ebnet

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Blood vessel tubulogenesis requires the formation of stable cell-to-cell contacts and the establishment of apicobasal polarity of vascular endothelial cells. Cell polarity is regulated by highly conserved cell polarity protein complexes such as the Par3-aPKC-Par6 complex and the CRB3-Pals1-PATJ complex, which are expressed by many different cell types and regulate various aspects of cell polarity. Here we describe a functional interaction of VEcadherin with the cell polarity protein Pals1. Pals1 directly interacts with VE-cadherin through a membrane-proximal motif in the cytoplasmic domain of VE-cadherin. VE-cadherin clusters Pals1 at cell-cell junctions. Mutating the Pals1-binding motif in VE-cadherin abrogates the ability of VE-cadherin to regulate apicobasal polarity and vascular lumen formation. In a similar way, deletion of the Par3-binding motif at the C-terminus of VE-cadherin impairs apicobasal polarity and vascular lumen formation. Our fndings indicate that the biological activity of VE-cadherin in regulating endothelial polarity and vascular lumen formation is mediated through its interaction with the two cell polarity proteins Pals1 and Par3.

Original languageEnglish
Pages (from-to)2811-2821
Number of pages11
JournalMolecular Biology of the Cell
Volume27
Issue number18
DOIs
Publication statusPublished - Sep 15 2016
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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