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A more recent version of this article appeared on June 1, 2006
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Submitted on November 21, 2005
Revised on March 24, 2006
Accepted on March 30, 2006
2
1 Integrin-mediated Stat1/3 Activation and Cell Migration
*Institute of Basic Medical Sciences and Departments of Physiology and Pharmacology, National Cheng Kung University Medical College, Tainan 701, Taiwan
Monitoring Editor: Carl-Henrik Heldin
Regulation of cell migration is an important step for the development of branching tubule morphogenesis in collagen gel. Here we showed that discoidin domain receptor (DDR) 1a/b inhibited collagen-induced tyrosine phosphorylation of Stat1/3 and cell migration triggered by 
2
1 integrin. Overexpression of DDR1a/b increased the interaction of DDR1 with SHP-2 and up-regulated the tyrosine phosphatase activity of SHP-2. Expression of catalytically inactive (C/S) SHP-2 in DDR1-transfected cells restored the tyrosine phosphorylation of Stat3 and cell migration. We demonstrated that the SH2-SH2 and PTP domains of SHP-2 were responsible for interaction with DDR1, and that both tyrosine phosphorylation sites 703 and 796 of DDR1 were essential for it to bind with SHP-2. Mutation of tyrosine 703 or 796 of DDR1 abolished the ability of DDR1 to inhibit the tyrosine phosphorylation of Stat1 and Stat3, and restored collagen-induced cell migration and hepatocyte growth factor (HGF)-induced branching tubulogenesis in collagen gel. Taken together, these results demonstrate that SHP-2 is required for the DDR1-induced suppression of Stat1 and Stat3 tyrosine phosphorylation, cell migration, and branching tubulogenesis.
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