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Ligand stimulation of CD155alpha inhibits cell adhesion and enhances cell migration in fibroblasts

Toshiyuki Oda1, Seii Ohka, Akio Nomoto

  • 1Department of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.

Biochemical and Biophysical Research Communications
|June 15, 2004
PubMed

Insights

CD155alpha, a poliovirus receptor, regulates cell adhesion and motility. Its ITIM motif, when phosphorylated, inhibits adhesion and enhances motility by recruiting SHP-2 phosphatase.

Area of Science:

  • Cell Biology
  • Immunology
  • Molecular Biology

Background:

  • CD155 (poliovirus receptor) is known to localize in cell-matrix and cell-cell junctions.
  • Its specific function in regulating cell adhesion and motility remained uninvestigated.

Purpose of the Study:

  • To investigate the role of CD155alpha in the regulation of cell adhesion and cell motility.
  • To identify the molecular mechanisms underlying CD155alpha's function in cell dynamics.

Main Methods:

  • Identification of a conserved immunoreceptor tyrosine-based inhibitory motif (ITIM) in human CD155alpha.
  • Analysis of tyrosine-phosphorylation of ITIM upon ligand binding (anti-CD155 mAb D171, poliovirus, DNAM-1/CD226).
  • Investigation of SHP-2 recruitment and its effect on focal adhesion kinase (FAK) and paxillin phosphorylation.

Main Results:

  • ITIM phosphorylation upon ligand binding led to SHP-2 recruitment.
  • CD155alpha stimulation inhibited cell adhesion and enhanced cell motility.
  • These effects were linked to ITIM phosphorylation by Src kinases and dephosphorylation of FAK and paxillin.
  • A Y398F mutation in ITIM or dominant-negative SHP-2 abolished these effects.

Conclusions:

  • CD155alpha plays a significant role in regulating cell adhesion and motility.
  • The ITIM motif and SHP-2 recruitment are critical for CD155alpha-mediated regulation of cell dynamics.
  • CD155alpha signaling pathway impacts focal adhesion turnover and cell migration.

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