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MBC in Press, published online ahead of print July 14, 2004
Mol. Biol. Cell 10.1091/mbc.E03-09-0640

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Submitted on September 3, 2003
Revised on July 2, 2004
Accepted on July 6, 2004

Crosstalk of Integrin {alpha}3{beta}1 and Tissue Factor in Cell Migration

Andrea Dorfleutner*{dagger}{ddagger}, Edith Hintermann{sect}{ddagger}, Takehiko Tarui{sect}, Yoshikazu Takada{sect}||, and Wolfram Ruf*¶

Departments of *Immunology and {sect}Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

Monitoring Editor: Martin A. Schwartz

In cancer and angiogenesis, coagulation-independent roles of tissue factor (TF) in cell migration are incompletely understood. Immobilized anti-TF extracellular domain antibodies induce cell spreading, but this phenomenon is epitope specific and not induced by anti-TF 5G9. Spreading on anti-TF is {beta}1 integrin-dependent, indicating functional interactions of the TF extracellular domain 5G9 epitope (a presumed integrin-binding site) and integrins. Recombinant TF extracellular domain supports adhesion of cells expressing {alpha}v{beta}3 or certain {beta}1 integrin heterodimers ({alpha}3{beta}1, {alpha}4{beta}1, {alpha}5{beta}1, {alpha}6{beta}1, {alpha}9{beta}1) and adhesion is blocked by specific antiintegrin antibodies or mutations in the integrin ligand-binding site. Whereas several studies have linked TF to cell migration, we here demonstrate that TF specifically regulates {alpha}3{beta}1-dependent migration on laminin 5. Expression of TF suppresses {alpha}3{beta}1-dependent migration, but only when the TF cytoplasmic domain is not phosphorylated. Suppression of migration can be reversed by 5G9, presumably by disrupting integrin interaction, or by the protease ligand VIIa, known to induce PAR-2-dependent phosphorylation of TF. In both cases, release of {alpha}3{beta}1 inhibition is prevented by mutation of critical phosphorylation sites in the TF cytoplasmic domain. Thus, TF influences integrin mediated migration through cooperative intraand extracellular interactions and phosphorylation regulates TF’s function in cell motility.

{ddagger}These authors contributed equally to this work

Present addresses: {dagger}The Mary Babb Randolph Cancer Center and the Department of Microbiology, Immunology, and Cell Biology, West Virginia University, Morgantown, WV 26506-9300; ||University of California Davis Medical Center, Research III, Suite 3300, 4645 2nd Avenue, Sacramento, CA 95817

Corresponding author. E-mail: ruf{at}scripps.edu




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