Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts

Exp Cell Res. 2004 Oct 15;300(1):121-33. doi: 10.1016/j.yexcr.2004.07.010.

Abstract

Endothelial cell-selective adhesion molecule (ESAM) is an immunoglobulin-like transmembrane protein associated with endothelial tight junctions (TJ). Based on a yeast two-hybrid screen, we have identified the membrane-associated guanylate kinase protein MAGI-1 as an intracellular binding partner of ESAM. MAGI-1 is a multidomain adaptor protein, which binds to transmembrane, cytoskeletal, and signaling molecules, and has been localized to tight junctions in epithelial cells. MAGI-1 associates with the very C-terminal sequence of ESAM most likely through a PDZ domain-mediated interaction. The direct interaction between ESAM and MAGI-1 was confirmed by pull-down experiments. The two proteins formed stable complexes in transfected Chinese hamster ovary (CHO) cells, which could be immunoisolated. We found MAGI-1 to be associated with cell-cell contacts in human umbilical vein endothelial cells (HUVECs) and in mouse endothelium, where it colocalizes with ESAM. In CHO cells, recruitment of MAGI-1 to cell contacts required the presence of ESAM. Hence, ESAM may be involved in anchoring MAGI-1 at endothelial tight junctions.

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Adaptor Proteins, Vesicular Transport / genetics
  • Adaptor Proteins, Vesicular Transport / isolation & purification
  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Alternative Splicing / genetics
  • Animals
  • Binding Sites / physiology
  • CHO Cells
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Cell Communication / physiology
  • Cell Line, Tumor
  • Cricetinae
  • Endothelial Cells
  • Endothelium, Vascular / metabolism
  • Guanylate Kinases
  • Humans
  • Macromolecular Substances
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Nucleoside-Phosphate Kinase / genetics
  • Nucleoside-Phosphate Kinase / isolation & purification
  • Nucleoside-Phosphate Kinase / metabolism*
  • Phylogeny
  • Protein Binding / physiology
  • Protein Structure, Tertiary / physiology
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Tight Junctions / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • CNKSR3 protein, human
  • Cell Adhesion Molecules
  • Esam protein, mouse
  • Macromolecular Substances
  • Membrane Proteins
  • Nucleoside-Phosphate Kinase
  • Guanylate Kinases
  • Magi1 protein, mouse

Associated data

  • GENBANK/AY497557