Ligand stimulation of CD155α inhibits cell adhesion and enhances cell migration in fibroblasts

被引：59

作者：

Oda, T ^{[1
]}

Ohka, S ^{[1
]}

Nomoto, A ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Med, Dept Microbiol, Tokyo, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 319卷 / 04期

关键词：

CD155; poliovirus receptor; SHP-2; ITIM; tyrosine-phosphorylation; cell adhesion; cell migration;

D O I：

10.1016/j.bbrc.2004.05.111

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CD155 (poliovirus receptor) localizes in cell-matrix adhesions and cell-cell junctions, but its role in the regulation of cell adhesion and cell motility has not been investigated. We identified a conserved immunoreceptor tyrosine-based inhibitory motif (ITIM) in the cytoplasmic domain of human CD155alpha. The ITIM was tyrosine-phosphorylated upon binding of anti-CD155 monoclonal antibody D171, poliovirus, and DNAM-1 (CD226) to human CD155alpha, and recruited SH2-domain-containing tyrosine phosphatase-2 (SHP-2). After CD155alpha stimulation with its ligands, cell adhesion was inhibited and cell motility was enhanced, effects that were associated with the phosphorylation of ITIM by Src kinases and accompanied by dephosphorylation of focal adhesion kinase and paxillin. These effects were abolished by introducing a point-mutation in Y398F into the ITIM of CD155alpha and by coexpression of a dominant negative SHP-2 mutant with CD155alpha. These results suggest that CD155alpha plays a role in the regulation of cell adhesion and cell motility. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：1253 / 1264

页数：12

共 51 条

[31] Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to αvβ3 integrin-containing membrane microdomains [J].